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Information on EC 1.1.3.15 - (S)-2-hydroxy-acid oxidase
for references in articles please use BRENDA:EC1.1.3.15
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.3 With oxygen as acceptor
1.1.3.15 (S)-2-hydroxy-acid oxidase
IUBMB Comments
A flavoprotein (FMN). Exists as two major isoenzymes; the A form preferentially oxidizes short-chain aliphatic hydroxy acids, and was previously listed as EC 1.1.3.1, glycolate oxidase; the B form preferentially oxidizes long-chain and aromatic hydroxy acids. The rat isoenzyme B also acts as EC 1.4.3.2, L-amino-acid oxidase.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 1.1.3.15
- venom
- snake
- catalase
-
biosensors
- laaos
-
electrode
- glyoxylate
- oxidases
-
electrochemical
-
amperometric
-
photorespiration
- oxalate
-
photorespiratory
- bothrops
-
d-amino
- crotalus
- hyperoxalurias
- viper
- antivenoms
- hydroxypyruvate
- microbodies
-
snakebite
-
crisp
- calloselasma
- cobra
- rhodostoma
- trimeresurus
-
thrombin-like
-
glyoxysomes
- agkistrodon
- kaouthia
- rattlesnake
- viridans
- adamanteus
-
screen-printed
-
flavocytochrome
-
malayan
-
elapid
-
fmn-dependent
- phosphomonoesterase
-
svmps
-
viperids
- hannah
- l-leu
- aerococcus
- daboia
- atrox
- drug development
- diagnostics
- medicine
- synthesis
-
bradykinin-potentiating
- analysis
- molecular biology
-
three-finger
- agriculture
-
nafion
showSynonyms
l-amino acid oxidase, glycolate oxidase, lactate oxidase, haox1, l-alpha-hydroxy acid oxidase, l-2-hydroxy acid oxidase, lchao, l-lactate monooxygenase, hydroxyacid oxidase 1, (l)-2-haox, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(S)-2-hydroxy-acid oxidase, peroxisomal
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EC 1.1.3.1
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formerly
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Glo1
GLO3
Glo4
glycolate oxidase
GO
GOX
HAO1
Hao2
HAOX1
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HAOX2
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HAOX3
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hydroxy-acid oxidase A
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hydroxy-acid oxidase B
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hydroxyacid oxidase 1
hydroxyacid oxidase A
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L-2-hydroxy acid oxidase
L-alpha-hydroxy acid oxidase
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L-lactate oxidase
lactate oxidase
LctO
long chain L-2-hydroxy acid oxidase 2
long-chain 2-hydroxy acid oxidase
LOX
oxidase, L-2-hydroxy acid
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additional information
the enzyme belongs to the FMN-dependent enzyme family
glycolate oxidase
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GOX
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L-2-hydroxy acid oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an (S)-2-hydroxy carboxylate + O2 = a 2-oxo carboxylate + H2O2
A flavoprotein, FMN. Exists as two major isoenzymes. The A form preferentially oxidizes short-chain aliphatic hydroxy acids, and was previously listed as EC 1.1.3.1, glycolate oxidase. The B form preferentially oxidizes long-chain and aromatic hydroxy acids. The rat isoenzyme B also acts as L-amino acid oxidase, EC 1.4.3.2
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an (S)-2-hydroxy carboxylate + O2 = a 2-oxo carboxylate + H2O2
the catalytic residue is Phe23, reaction mechanism
an (S)-2-hydroxy carboxylate + O2 = a 2-oxo carboxylate + H2O2
the pH affects the kinetic steps of the catalytic mechanism of human glycolate oxidase, the enzyme shows a ping-pong bi-bi kinetic mechanism between pH 6.0 and 10.0, overview. Formation of the enzyme-substrate complex suggests the presence of a protonated group participating in substrate binding
an (S)-2-hydroxy carboxylate + O2 = a 2-oxo carboxylate + H2O2
reaction mechanism, quantum mechanics/molecular mechanics calculations and molecular dynamics simulations, overview. LCHAO-catalyzed dehydrogenation of L-lactate is a stepwise catalytic reaction in a hydride transfer mechanism but not a carbanion mechanism. In contrast to the wild-type enzyme, the mutant Y129F LCHAO catalyzes the oxidation of L-lactate in one step
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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oxidative decarboxylation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
photorespiration I
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SYSTEMATIC NAME
IUBMB Comments
(S)-2-hydroxy-acid:oxygen 2-oxidoreductase
A flavoprotein (FMN). Exists as two major isoenzymes; the A form preferentially oxidizes short-chain aliphatic hydroxy acids, and was previously listed as EC 1.1.3.1, glycolate oxidase; the B form preferentially oxidizes long-chain and aromatic hydroxy acids. The rat isoenzyme B also acts as EC 1.4.3.2, L-amino-acid oxidase.
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CAS REGISTRY NUMBER
COMMENTARY
9037-63-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-2-hydroxybutanoate + 2,6-dichlorophenolindophenol
2-oxobutanoate + reduced 2,6-dichlorophenolindophenol
Substrates: preferred substrate
Products: -
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?
(R)-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
Substrates: preferred substrate
Products: -
Products: -
?
2-hydroxy-3-methylvalerate + O2
?
-
Substrates: A95G-mutant
Products: -
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?
2-hydroxybutanoate + bromopyruvate + ?
bromolactate + pyruvate + ?
-
Substrates: transhydrogenation reaction
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?
2-hydroxybutyrate + O2
?
-
Substrates: wild-type and A95G-mutant
Products: -
Products: -
?
2-hydroxycaproate + O2
2-oxocaproate + H2O2
Substrates: -
Products: -
Products: -
?
2-hydroxycaprylate + O2
2-oxocaprylate + H2O2
Substrates: -
Products: -
Products: -
?
2-hydroxydodecanoate + O2
2-oxododecanoate + H2O2
Substrates: -
Products: -
Products: -
?
2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
Substrates: -
Products: -
Products: -
?
2-hydroxyoctanoate + 2,6-dichlorophenolindophenol
2-oxo-octanoate + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
r
2-hydroxyoctanoate + O2
2-oxooctanoate + H2O2
-
Substrates: substrates for isoenzymes HAOX1, HAOX2, preferred substrate for isoenzyme HAOX3
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Products: -
?
2-hydroxyvalerate + O2
?
-
Substrates: wild-type and A95G-mutant
Products: -
Products: -
?
D-lactate + O2
pyruvate + H2O2
-
Substrates: traces of activity
Products: -
Products: -
?
DL-2-hydroxy-3-butynoate + O2
2-oxo-3-butynoate + H2O2
-
Substrates: good substrate, but inactivation after 25 turnovers
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Products: -
?
DL-2-hydroxy-3-heptynoate + O2
2-oxo-3-heptynoate + H2O2
-
Substrates: 86% of the activity compared to DL-2-hydroxybutyrate
Products: -
Products: -
?
DL-2-hydroxy-3-hexynoate + O2
2-oxo-3-hexynoate + H2O2
-
Substrates: 65% of the activity compared to DL-2-hydroxybutyrate
Products: -
Products: -
?
DL-2-hydroxy-3-octynoate + O2
2-oxo-3-octynoate + H2O2
-
Substrates: 70% of the activity compared to DL-2-hydroxybutyrate
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Products: -
?
DL-2-hydroxy-3-pentynoate + O2
2-oxo-3-pentynoate + H2O2
-
Substrates: 2fold higher activity compared to DL-2-hydroxybutyrate
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Products: -
?
DL-2-hydroxy-4-methylmercaptobutyrate + 2,6-dichlorophenolindophenol
2-oxo-4-methylmercaptobutyrate + reduced 2,6-dichlorophenolindophenol
-
Substrates: good substrate for long chain oxidase, low activity for short chain oxidase
Products: -
Products: -
?
DL-2-hydroxy-4-methylthiobutanoic acid + 2,6-dichlorophenolindophenol
2-oxo-4-methylthiobutanoic acid + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
DL-2-hydroxybutyrate + 2,4-dinitrophenylhydrazine
2-oxobutyrate 2,4-dinitrophenylhydrazone + ?
-
Substrates: low activity
Products: -
Products: -
?
DL-2-hydroxybutyrate + 2,6-dichlorophenolindophenol
2-oxobutyrate + reduced 2,6-dichlorophenolindophenol
DL-2-hydroxycaproate + 2,6-dichlorophenolindophenol
2-oxocaproate + reduced 2,6-dichlorophenolindophenol
-
Substrates: low activity for short chain oxidase, moderate activity for long chain oxidase
Products: -
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?
DL-2-hydroxydecanoate + 2,6-dichlorophenolindophenol
2-oxodecanoate + reduced 2,6-dichlorophenolindophenol
-
Substrates: good substrate for long chain oxidase, traces of activity for short chain oxidase
Products: -
Products: -
?
DL-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
Substrates: -
Products: -
Products: -
?
DL-2-hydroxyisovalerate + 2,4-dinitrophenylhydrazine
2-oxoisovalerate 2,4-dinitrophenylhydrazone + ?
-
Substrates: very low activity
Products: -
Products: -
?
DL-2-hydroxyisovalerate + 2,6-dichlorophenolindophenol
2-oxoisovalerate + reduced 2,6-dichlorophenolindophenol
-
Substrates: no activity for short chain oxidase, moderate activity for long chain oxidase
Products: -
Products: -
?
DL-2-hydroxyoctanoate + 2,6-dichlorophenolindophenol
2-oxooctanoate + reduced 2,6-dichlorophenolindophenol
-
Substrates: good substrate for long chain oxidase, no activity for short chain oxidase
Products: -
Products: -
?
DL-2-hydroxyvalerate + 2,6-dichlorophenolindophenol
2-oxovalerate + reduced 2,6-dichlorophenolindophenol
-
Substrates: low activity for short chain oxidase, moderate activity for long chain oxidase
Products: -
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?
DL-3-indolelactate + 2,6-dichlorophenolindophenol
3-indolepyruvate + reduced 2,6-dichlorophenolindophenol
-
Substrates: good substrate for long chain oxidase, no activity for short chain oxidase
Products: -
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?
DL-3-methoxy-4-hydroxymandelate + 2,6-dichlorophenolindophenol
(3-methoxy-4-hydroxyphenyl)pyruvate + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
DL-beta-phenyllactate + 2,6-dichlorophenolindophenol
phenylpyruvate + reduced 2,6-dichlorophenolindophenol
-
Substrates: no activity for short chain oxidase
Products: -
Products: -
?
DL-mandelate + 2,6-dichlorophenolindophenol
oxo(phenyl)acetic acid + reduced 2,6-dichlorophenolindophenol
-
Substrates: low activity
Products: -
Products: -
?
DL-mandelate + O2
phenylglyoxylic acid + H2O2
-
Substrates: the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
Products: -
Products: -
?
DL-p-hydroxy-beta-phenyllactate + 2,6-dichlorophenolindophenol
(4-hydroxyphenyl)pyruvate + reduced 2,6-dichlorophenolindophenol
-
Substrates: no activity for short chain oxidase
Products: -
Products: -
?
DL-p-hydroxymandelate + O2
?
-
Substrates: the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
Products: -
Products: -
?
DL-phenyllactate + O2
phenylpyruvate + H2O2
-
Substrates: -
Products: -
Products: -
?
DL-vinylglycolate + O2
2-oxo-3-butenoic acid + H2O2
-
Substrates: 90% of the activity compared to DL-2-hydroxybutyrate
Products: -
Products: -
?
glycolate + 2,4-dinitrophenylhydrazine
glyoxylate 2,4-dinitrophenylhydrazone + ?
-
Substrates: best substrate tested
Products: -
Products: -
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
glycolate + ferricyanide
glyoxylate + ferrocyanide
-
Substrates: -
Products: -
Products: -
?
glycolate + phenazine methosulfate
glyoxylate + reduced phenazine methosulfate
Substrates: -
Products: -
Products: -
?
glycolate + phenylhydrazine
glyoxylate phenylhydrazone + H2O
Substrates: -
Products: -
Products: -
?
glyoxylate thiohemiacetals + O2
? + H2O2
-
Substrates: possible natural substrates, i.e. glyoxylate thiohemiacetals of coemzyme A, D-phosphopantetheine, D-pantetheine, N-acetylcysteamine, 2-mercaptoethanol, DL-dihydrolipoate, propane-1,3-dithiol
Products: -
Products: -
?
isoleucic acid + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
L-2-hydroxy octanoate + O2
2-oxo-octanoate + H2O2
Substrates: -
Products: -
Products: -
?
L-2-hydroxy palmitate + O2
2-oxo-palmitate + H2O2
Substrates: -
Products: -
Products: -
?
L-2-hydroxy-4-methylthiobutanoic acid + O2
3-(methylthio)propanoate + HCO3-
-
Substrates: oxidative decarboxylation
Products: -
Products: -
?
L-2-hydroxy-beta-methylvalerate + 2,6-dichlorophenolindophenol
3-methyl-2-oxopentanoate + reduced 2,6-dichlorophenolindophenol
L-2-hydroxyisocaproate + 2,4-dinitrophenylhydrazine
2-oxoisocaproate 2,4-dinitrophenylhydrazone + ?
-
Substrates: -
Products: -
Products: -
?
L-2-hydroxyisocaproate + 2,6-dichlorophenolindophenol
2-oxoisocaproate + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
L-2-hydroxyisocaproate + O2
4-methyl-2-oxopentanoate + H2O2
-
Substrates: 100% activity with long chain oxidase, 32% activity with short chain oxidase
Products: -
Products: -
r
L-4-chloromandelate + O2
?
-
Substrates: the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
Products: -
Products: -
?
L-4-fluoromandelate + O2
?
-
Substrates: the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
Products: -
Products: -
?
L-4-methoxymandelate + O2
?
-
Substrates: the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
Products: -
Products: -
?
L-4-methylmandelate + O2
?
-
Substrates: the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
Products: -
Products: -
?
L-4-nitromandelate + O2
?
-
Substrates: the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
Products: -
Products: -
?
L-4-trifluoromethylmandelate + O2
?
-
Substrates: the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
Products: -
Products: -
?
L-alpha-hydroxy-isovalerate + O2
3-methyl-2-oxobutanoate + H2O2
-
Substrates: -
Products: -
Products: -
r
L-lactate + 2,4-dinitrophenylhydrazine
pyruvate 2,4-dinitrophenylhydrazone + ?
-
Substrates: very low activity
Products: -
Products: -
?
L-lactate + phenazine methosulfate
? + reduced phenazine methosulfate
Substrates: -
Products: -
Products: -
?
L-lactate + phenylhydrazine
pyruvate phenylhydrazone + H2O
Substrates: -
Products: -
Products: -
?
L-leucine + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
L-mandelate + 2,6-dichlorophenolindophenol
oxo(phenyl)acetic acid + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
L-phenyllactate + 2,6-dichlorophenolindophenol
phenylpyruvate + reduced 2,6-dichlorophenolindophenol
mandelate + O2
phenylpyruvate + H2O2
Substrates: oxidation of an L-2-hydroxy acid to a 2-oxoacid, model for the binding of L-mandelate into the active site, overview
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?
thiol-glyoxylate adducts + O2
an oxalyl thioester + H2O2
-
Substrates: may be the physiological substrates
Products: -
Products: -
?
valic acid + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
(S)-lactate + O2
acetate + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
(S)-lactate + O2
acetate + CO2 + H2O
-
Substrates: glucose-repressible lactate oxidase is likely responsible for H2O2 production
Products: -
Products: -
?
(S)-lactate + O2
pyruvate + H2O2
-
Substrates: no decarboxylation
Products: -
Products: -
?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
Substrates: -
Products: -
Products: -
?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
-
Substrates: substrates for isoenzymes HAOX1, HAOX2
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Products: -
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Substrates: -
Products: -
Products: -
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Substrates: -
Products: -
Products: -
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Substrates: -
Products: -
Products: -
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Substrates: -
Products: -
Products: -
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Substrates: -
Products: -
Products: -
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Substrates: -
Products: -
Products: -
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Substrates: -
Products: -
Products: -
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Substrates: -
Products: -
Products: -
?
D-2 -hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
Substrates: 48% of the activity compared to glycolate
Products: -
Products: -
?
D-2 -hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
Substrates: liver enzyme is much less active with C4 or C5 alpha-hydroxy acids but as active as with glycolate
Products: -
Products: -
?
DL-2-hydroxybutyrate + 2,6-dichlorophenolindophenol
2-oxobutyrate + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
DL-2-hydroxybutyrate + 2,6-dichlorophenolindophenol
2-oxobutyrate + reduced 2,6-dichlorophenolindophenol
-
Substrates: low activity for long chain oxidase, no activity for short chain oxidase
Products: -
Products: -
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
Substrates: 68% of the activity compared to glycolate
Products: -
Products: -
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
Substrates: -
Products: -
Products: -
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
Substrates: best substrate tested
Products: -
Products: -
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
Substrates: higher affinity with C5 and C6 hydroxy acids
Products: -
Products: -
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
Substrates: best substrate tested
Products: -
Products: -
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
Substrates: -
Products: -
Products: -
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
Substrates: low activity
Products: -
Products: -
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
-
Substrates: -
Products: -
Products: -
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
-
Substrates: low activity
Products: -
Products: -
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
Substrates: 39% of the activity compared to glycolate
Products: -
Products: -
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
Substrates: -
Products: -
Products: -
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
Substrates: low activity
Products: -
Products: -
?
DL-3-chlorolactate + O2
3-chloropyruvate + H2O2
-
Substrates: -
Products: -
Products: -
?
DL-3-chlorolactate + O2
3-chloropyruvate + H2O2
-
Substrates: best substrate tested
Products: -
Products: -
?
glycerate + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
Substrates: highest activity for short chain oxidase, no activity for long chain oxidase
Products: -
Products: -
?
glycolate + acceptor
glyoxylate + reduced acceptor
Substrates: -
Products: -
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?
glycolate + acceptor
glyoxylate + reduced acceptor
-
Substrates: -
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?
glycolate + O2
glyoxylate + H2O2
-
Substrates: highest activity for isoenzyme HAOX1, no activity for isoenzymes HAOX2, HAOX3
Products: -
Products: -
?
glycolate + O2
glyoxylate + H2O2
-
Substrates: substrate for isoenzyme A
Products: -
Products: -
?
glycolate + O2
glyoxylate + H2O2
-
Substrates: the catalytic adduct is formed by hydrogen abstraction from the re-face of glycolate
Products: -
Products: -
?
glycolate + O2
glyoxylate + H2O2
Substrates: best substrate
Products: -
Products: -
?
glycolate + O2
glyoxylate + H2O2
-
Substrates: -
Products: -
Products: -
?
glycolate + O2
glyoxylate + H2O2
-
Substrates: substrate for isoenzyme A
Products: -
Products: -
?
glycolate + O2
glyoxylate + H2O2
-
Substrates: isoenzyme A utilizes short chain aliphatic hydroxy acids, isoenzyme B utilizes long-chain and aromatic hydroxyacids, that may also utilize L-amino acids
Products: -
Products: -
?
glycolate + O2
glyoxylate + H2O2
-
Substrates: preference for long chain substrates, more efficient hydroxy acid oxidase than an amino acid oxidase
Products: -
Products: -
?
glycolate + O2
glyoxylate + H2O2
-
Substrates: -
Products: -
Products: -
?
glycolate + O2
glyoxylate + H2O2
-
Substrates: -
Products: -
Products: -
?
glyoxylate + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
glyoxylate + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
glyoxylate + O2
? + H2O2
-
Substrates: substrate for isoenzyme HAOX1
Products: -
Products: -
?
glyoxylate + O2
? + H2O2
-
Substrates: 26% of the activity compared to glycolate
Products: -
Products: -
?
glyoxylate + O2
? + H2O2
Substrates: -
Products: -
Products: -
?
glyoxylate + O2
? + H2O2
-
Substrates: in the absence of any nucleophile less than 2% of the activity compared to glycolate
Products: -
Products: -
?
glyoxylate + O2
? + H2O2
-
Substrates: 40% of the activity compared to glycolate
Products: -
Products: -
?
L-2-hydroxy-beta-methylvalerate + 2,6-dichlorophenolindophenol
3-methyl-2-oxopentanoate + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
L-2-hydroxy-beta-methylvalerate + 2,6-dichlorophenolindophenol
3-methyl-2-oxopentanoate + reduced 2,6-dichlorophenolindophenol
-
Substrates: no activity for short chain oxidase
Products: -
Products: -
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
Substrates: substrate for isoenzyme B
Products: -
Products: -
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
Substrates: -
Products: -
Products: -
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
Substrates: best substrate tested
Products: -
Products: -
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
Substrates: substrate for isoenzyme B
Products: -
Products: -
?
L-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
L-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
L-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
-
Substrates: lower activity for preparation from "heavy" mitochondria
Products: -
Products: -
?
L-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
-
Substrates: very low activity
Products: -
Products: -
?
L-lactate + O2
pyruvate + H2O2
Substrates: -
Products: -
Products: -
?
L-lactate + O2
pyruvate + H2O2
-
Substrates: 28% of the activity compared to glycolate
Products: -
Products: -
?
L-lactate + O2
pyruvate + H2O2
Substrates: -
Products: -
Products: -
?
L-lactate + O2
pyruvate + H2O2
-
Substrates: yoghurt mixed and homogenized in water, filtered (20-25 microm), this sample injected into the luminometer measuring cell containing the lactate biosensor-system
Products: -
Products: -
?
L-lactate + O2
pyruvate + H2O2
-
Substrates: high activity, does not act on D-lactate
Products: -
Products: -
?
L-mandelate + O2
?
-
Substrates: A95G-mutant is also reactive
Products: -
Products: -
?
L-mandelate + O2
?
-
Substrates: the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
Products: -
Products: -
?
L-phenyllactate + 2,6-dichlorophenolindophenol
phenylpyruvate + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
L-phenyllactate + 2,6-dichlorophenolindophenol
phenylpyruvate + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
lactate + O2
pyruvate + H2O2
-
Substrates: lactate detection in beer samples
Products: H2O2 oxidizes Prussian Blue on an electrode, the concomitant electron flow is measured
Products: H2O2 oxidizes Prussian Blue on an electrode, the concomitant electron flow is measured
?
additional information
?
-
Substrates: isozyme lHAOX1 displays the highest activity with the long-chain fatty acid 2-hydroxyhexadecanoic acid (2-hydroxypalmitic acid) and has intermediate activity with 2-hydroxyhexanoic acid (2-hydroxycaproic acid), 2-hydroxyoctanoic acid (2-hydroxycaprylic acid), and the short-chain hydroxyacid L-lactate. With much lower activity, it can also use glycolate, leucic acid, valic acid, and isoleucic acid as substrates. No activity with 2-hydroxyhexadecanoic acid and D-lactate
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme lHAOX1 displays the highest activity with the long-chain fatty acid 2-hydroxyhexadecanoic acid (2-hydroxypalmitic acid) and has intermediate activity with 2-hydroxyhexanoic acid (2-hydroxycaproic acid), 2-hydroxyoctanoic acid (2-hydroxycaprylic acid), and the short-chain hydroxyacid L-lactate. With much lower activity, it can also use glycolate, leucic acid, valic acid, and isoleucic acid as substrates. No activity with 2-hydroxyhexadecanoic acid and D-lactate
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme lHAOX1 displays the highest activity with the long-chain fatty acid 2-hydroxyhexadecanoic acid (2-hydroxypalmitic acid) and has intermediate activity with 2-hydroxyhexanoic acid (2-hydroxycaproic acid), 2-hydroxyoctanoic acid (2-hydroxycaprylic acid), and the short-chain hydroxyacid L-lactate. With much lower activity, it can also use glycolate, leucic acid, valic acid, and isoleucic acid as substrates. No activity with 2-hydroxyhexadecanoic acid and D-lactate
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme lHAOX2 exhibits the highest activity with leucic acid. It shows intermediate activity with 2-hydroxyhexanoic acid and 2-hydroxyoctanoic acid. lHAOX2 displays lower activity with 2-hydroxydodecanoic acid, valic acid, and isoleucic acid and poor activity with glycolate and L-lactate. No activity with 2-hydroxyhexadecanoic acid and D-lactate
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme lHAOX2 exhibits the highest activity with leucic acid. It shows intermediate activity with 2-hydroxyhexanoic acid and 2-hydroxyoctanoic acid. lHAOX2 displays lower activity with 2-hydroxydodecanoic acid, valic acid, and isoleucic acid and poor activity with glycolate and L-lactate. No activity with 2-hydroxyhexadecanoic acid and D-lactate
Products: -
Products: -
?
additional information
?
-
Substrates: isozyme lHAOX2 exhibits the highest activity with leucic acid. It shows intermediate activity with 2-hydroxyhexanoic acid and 2-hydroxyoctanoic acid. lHAOX2 displays lower activity with 2-hydroxydodecanoic acid, valic acid, and isoleucic acid and poor activity with glycolate and L-lactate. No activity with 2-hydroxyhexadecanoic acid and D-lactate
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: D-alanine, pyruvate, D-glucose, L-alanine, ethanol and L-lactate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: oxalate, acetate, pyruvate, glycerol, propionate, succinate, fumarate, malate, maleate, tartrate, oxaloacetate, 2-oxoglutarate, glycocol,L-alanine, serine, glutamate, ascorbate, glucose, and fructose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: glyoxylate. Enzyme also catalyzes the oxidation of short-chain alcohols, reaction of EC 1.1.3.13
Products: -
Products: -
?
additional information
?
-
-
Substrates: interaction of Rice dwarf virus, RDV, outer capsid P8 protein with rice glycolate oxidase mediates relocalization of P8, GOX may play important roles in RDV targeting into the replication site of host cells, overview
Products: -
Products: -
?
additional information
?
-
Substrates: GLO is a typical photorespiratory enzyme and it exerts a strong regulation over photosynthesis, possibly through a feed-back inhibition on Rubisco activase, the glyoxylate cycle may be partially activated to compensate for the photorespiratory glyoxylate when GLO is suppressed in rice
Products: -
Products: -
?
additional information
?
-
-
Substrates: GLO is a typical photorespiratory enzyme and it exerts a strong regulation over photosynthesis, possibly through a feed-back inhibition on Rubisco activase, the glyoxylate cycle may be partially activated to compensate for the photorespiratory glyoxylate when GLO is suppressed in rice
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is involved in the photorespiration process
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is not able to metabolize D-lactate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is not able to metabolize D-lactate
Products: -
Products: -
?
additional information
?
-
Substrates: long-chain L-alpha-hydroxy acid oxidase (LCHAO) is a FMN-dependent oxidase that dehydrogenates L-alpha-hydroxy acids to oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the photorespiration process
Products: -
Products: -
?
additional information
?
-
-
Substrates: energy-yielding metabolism can be described as follows: as long as glucose is available, approximatelyone-fourth of the pyruvate formed is converted to acetate by the sequential action of pyruvate oxidase and acetate kinase with acquisition of additional ATP. The rest of the pyruvate is reduced by lactate dehydrogenase to form lactate, with partial achievement of redox balance. The lactate is oxidized by lactate oxidase back to pyruvate, which is converted to acetate as described above; and the sequential reactions mentioned above continue to occur as long as lactate is present
Products: -
Products: -
?
additional information
?
-
-
Substrates: energy-yielding metabolism can be described as follows: as long as glucose is available, approximatelyone-fourth of the pyruvate formed is converted to acetate by the sequential action of pyruvate oxidase and acetate kinase with acquisition of additional ATP. The rest of the pyruvate is reduced by lactate dehydrogenase to form lactate, with partial achievement of redox balance. The lactate is oxidized by lactate oxidase back to pyruvate, which is converted to acetate as described above; and the sequential reactions mentioned above continue to occur as long as lactate is present
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-hydroxycaproate + O2
2-oxocaproate + H2O2
Substrates: -
Products: -
Products: -
?
2-hydroxycaprylate + O2
2-oxocaprylate + H2O2
Substrates: -
Products: -
Products: -
?
2-hydroxyoctanoate + O2
2-oxooctanoate + H2O2
-
Substrates: substrates for isoenzymes HAOX1, HAOX2, preferred substrate for isoenzyme HAOX3
Products: -
Products: -
?
D-lactate + O2
pyruvate + H2O2
-
Substrates: traces of activity
Products: -
Products: -
?
DL-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
Substrates: -
Products: -
Products: -
?
glycolate + acceptor
glyoxylate + reduced acceptor
Substrates: -
Products: -
Products: -
?
glyoxylate thiohemiacetals + O2
? + H2O2
-
Substrates: possible natural substrates, i.e. glyoxylate thiohemiacetals of coemzyme A, D-phosphopantetheine, D-pantetheine, N-acetylcysteamine, 2-mercaptoethanol, DL-dihydrolipoate, propane-1,3-dithiol
Products: -
Products: -
?
L-2-hydroxy-4-methylthiobutanoic acid + O2
3-(methylthio)propanoate + HCO3-
-
Substrates: oxidative decarboxylation
Products: -
Products: -
?
thiol-glyoxylate adducts + O2
an oxalyl thioester + H2O2
-
Substrates: may be the physiological substrates
Products: -
Products: -
?
(S)-lactate + O2
pyruvate + H2O2
-
Substrates: no decarboxylation
Products: -
Products: -
?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
Substrates: -
Products: -
Products: -
?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
-
Substrates: substrates for isoenzymes HAOX1, HAOX2
Products: -
Products: -
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Substrates: -
Products: -
Products: -
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Substrates: -
Products: -
Products: -
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Substrates: -
Products: -
Products: -
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Substrates: -
Products: -
Products: -
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Substrates: -
Products: -
Products: -
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Substrates: -
Products: -
Products: -
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Substrates: -
Products: -
Products: -
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Substrates: -
Products: -
Products: -
?
D-2 -hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
Substrates: 48% of the activity compared to glycolate
Products: -
Products: -
?
D-2 -hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
Substrates: liver enzyme is much less active with C4 or C5 alpha-hydroxy acids but as active as with glycolate
Products: -
Products: -
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
Substrates: 68% of the activity compared to glycolate
Products: -
Products: -
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
Substrates: -
Products: -
Products: -
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
Substrates: best substrate tested
Products: -
Products: -
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
Substrates: higher affinity with C5 and C6 hydroxy acids
Products: -
Products: -
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
Substrates: best substrate tested
Products: -
Products: -
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
Substrates: -
Products: -
Products: -
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
Substrates: low activity
Products: -
Products: -
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
-
Substrates: -
Products: -
Products: -
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
-
Substrates: low activity
Products: -
Products: -
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
Substrates: 39% of the activity compared to glycolate
Products: -
Products: -
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
Substrates: -
Products: -
Products: -
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
Substrates: low activity
Products: -
Products: -
?
glycolate + O2
glyoxylate + H2O2
-
Substrates: highest activity for isoenzyme HAOX1, no activity for isoenzymes HAOX2, HAOX3
Products: -
Products: -
?
glycolate + O2
glyoxylate + H2O2
-
Substrates: substrate for isoenzyme A
Products: -
Products: -
?
glycolate + O2
glyoxylate + H2O2
-
Substrates: -
Products: -
Products: -
?
glycolate + O2
glyoxylate + H2O2
-
Substrates: substrate for isoenzyme A
Products: -
Products: -
?
glycolate + O2
glyoxylate + H2O2
-
Substrates: isoenzyme A utilizes short chain aliphatic hydroxy acids, isoenzyme B utilizes long-chain and aromatic hydroxyacids, that may also utilize L-amino acids
Products: -
Products: -
?
glycolate + O2
glyoxylate + H2O2
-
Substrates: preference for long chain substrates, more efficient hydroxy acid oxidase than an amino acid oxidase
Products: -
Products: -
?
glycolate + O2
glyoxylate + H2O2
-
Substrates: -
Products: -
Products: -
?
glyoxylate + O2
? + H2O2
-
Substrates: substrate for isoenzyme HAOX1
Products: -
Products: -
?
glyoxylate + O2
? + H2O2
-
Substrates: 26% of the activity compared to glycolate
Products: -
Products: -
?
glyoxylate + O2
? + H2O2
-
Substrates: in the absence of any nucleophile less than 2% of the activity compared to glycolate
Products: -
Products: -
?
glyoxylate + O2
? + H2O2
-
Substrates: 40% of the activity compared to glycolate
Products: -
Products: -
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
Substrates: substrate for isoenzyme B
Products: -
Products: -
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
Substrates: -
Products: -
Products: -
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
Substrates: best substrate tested
Products: -
Products: -
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
Substrates: substrate for isoenzyme B
Products: -
Products: -
?
L-lactate + O2
pyruvate + H2O2
Substrates: -
Products: -
Products: -
?
L-lactate + O2
pyruvate + H2O2
-
Substrates: 28% of the activity compared to glycolate
Products: -
Products: -
?
L-lactate + O2
pyruvate + H2O2
-
Substrates: yoghurt mixed and homogenized in water, filtered (20-25 microm), this sample injected into the luminometer measuring cell containing the lactate biosensor-system
Products: -
Products: -
?
L-lactate + O2
pyruvate + H2O2
-
Substrates: high activity, does not act on D-lactate
Products: -
Products: -
?
lactate + O2
pyruvate + H2O2
-
Substrates: lactate detection in beer samples
Products: H2O2 oxidizes Prussian Blue on an electrode, the concomitant electron flow is measured
Products: H2O2 oxidizes Prussian Blue on an electrode, the concomitant electron flow is measured
?
additional information
?
-
-
Substrates: interaction of Rice dwarf virus, RDV, outer capsid P8 protein with rice glycolate oxidase mediates relocalization of P8, GOX may play important roles in RDV targeting into the replication site of host cells, overview
Products: -
Products: -
?
additional information
?
-
Substrates: GLO is a typical photorespiratory enzyme and it exerts a strong regulation over photosynthesis, possibly through a feed-back inhibition on Rubisco activase, the glyoxylate cycle may be partially activated to compensate for the photorespiratory glyoxylate when GLO is suppressed in rice
Products: -
Products: -
?
additional information
?
-
-
Substrates: GLO is a typical photorespiratory enzyme and it exerts a strong regulation over photosynthesis, possibly through a feed-back inhibition on Rubisco activase, the glyoxylate cycle may be partially activated to compensate for the photorespiratory glyoxylate when GLO is suppressed in rice
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is involved in the photorespiration process
Products: -
Products: -
?
additional information
?
-
Substrates: long-chain L-alpha-hydroxy acid oxidase (LCHAO) is a FMN-dependent oxidase that dehydrogenates L-alpha-hydroxy acids to oxo acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the photorespiration process
Products: -
Products: -
?
additional information
?
-
-
Substrates: energy-yielding metabolism can be described as follows: as long as glucose is available, approximatelyone-fourth of the pyruvate formed is converted to acetate by the sequential action of pyruvate oxidase and acetate kinase with acquisition of additional ATP. The rest of the pyruvate is reduced by lactate dehydrogenase to form lactate, with partial achievement of redox balance. The lactate is oxidized by lactate oxidase back to pyruvate, which is converted to acetate as described above; and the sequential reactions mentioned above continue to occur as long as lactate is present
Products: -
Products: -
?
additional information
?
-
-
Substrates: energy-yielding metabolism can be described as follows: as long as glucose is available, approximatelyone-fourth of the pyruvate formed is converted to acetate by the sequential action of pyruvate oxidase and acetate kinase with acquisition of additional ATP. The rest of the pyruvate is reduced by lactate dehydrogenase to form lactate, with partial achievement of redox balance. The lactate is oxidized by lactate oxidase back to pyruvate, which is converted to acetate as described above; and the sequential reactions mentioned above continue to occur as long as lactate is present
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
both FMN and FAD, with FAD 46.8% of the activity with FMN
FMN
-
three-residue insertion of loop 4 in isozyme beta2 influences ionisation state of FMN
FMN
-
both FMN and FAD, with FAD 46.8% of the activity with FMN
FMN
the enzyme contains a GOX-like-riboflavin-5'-phosphate conserved domain
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
exposure of cells to mM copper sulfate, strong induction. Highest induction at 0.3 mM, about 16-fold increase in activity. Identification of a copper-response element in the 5'-region of the LctO gene
CuSO4
induces copper regulated promoter, upregulates LctO 17fold (2D gel)
additional information
additional information
Zn2+, Fe2+, Ni2+, Mn2+, and Ca2+ have no significant effect on lctO expression
additional information
-
Zn2+, Fe2+, Ni2+, Mn2+, and Ca2+ have no significant effect on lctO expression
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-oxoisocaproate
-
non-competitive inhibition at 5 mM, most active inhibitor of 2-keto acids, oxidation of 2-hydroxybutyrate most sensitive
3-decyl-2,5-dioxo-4-hydroxy-3-pyrroline
-
bound to the active site in the three-dimensional structure
4-carboxy-5-(1-pentyl)hexylsulfanyl-1,2,3-triazole
-
bound to the active site in the three-dimensional structure
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
arsenate
-
inhibition of glycolate-ferricyanide or glyoxylate-ferricyanide assay above 0.1 M
Atebrin
-
long chain oxidase, 72-76% inhibition at 1 mM, short chain oxidase: 68-76% inhibition at 1 mM
Cibacron blue 3GA
-
at a concentration higher than 0.001 mM is a normal competitive inhibitor, at concentrations below 0.001 mM the inhibition is time-, dye- and pH-dependent
DL-2-hydroxy-3-butynoate
-
irreversible inactivation after 25 turnovers, covalent addition to the coenzyme
DL-beta-Phenyllactate
-
short chain oxidase: 10% inhibition of glycolate oxidation, 81% inhibition of L-2-hydroxisocaproate oxidation at 10 mM
DL-Lipoate
-
long chain oxidase, 35% inhibition at 0.24 mM, short chain oxidase: 46-52% inhibition at 0.01 mM
3-benzyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-benzyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-ethoxy-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-ethoxy-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-ethyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-ethyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-fluorophenyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
35% inhibition at 0.010 mM
4-chloromercuribenzoate
-
long chain oxidase, 29-42% inhibition at 0.001 mM, short chain oxidase: 70-75% inhibition at 0.001 mM
4-[(2'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(3'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-carbamoylbiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-carbamoylbiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-carboxybiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-cyanobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-fluorobiphenyl-2-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-fluorobiphenyl-4-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[2-(4'-fluorobiphenyl-3-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[2-(4'-fluorobiphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[[4'-(2-amino-2-oxoethyl)biphenyl-3-yl]methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[[4'-(2-amino-2-oxoethyl)biphenyl-3-yl]methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
-
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
-
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(propan-2-yl)-1H-pyrazole-5-carboxylic acid
-
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(propan-2-yl)-1H-pyrazole-5-carboxylic acid
-
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-phenyl-1H-pyrazole-5-carboxylic acid
-
-
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-phenyl-1H-pyrazole-5-carboxylic acid
-
-
iodoacetate
-
long chain oxidase, 31-36% inhibition at 0.1 mM, short chain oxidase: no inhibition
KCN
-
30% inhibition of L-2-hydroxyisocaproate oxidation at 1 mM, 91% inhibition of glycolate oxidation at 1 mM
o-Iodosobenzoate
-
long chain oxidase, 95-100% inhibition at 0.1 mM, short chain oxidase: no inhibition
oxalate
-
mixed-type non-competitive inhibition, increasing inhibitory effects as the number of carbons in aliphatic chains decreases
oxalate
-
18% inhibition of glycolate oxidation, 71% inhibition of glyoxylate oxidation at 0.03 mM
phosphate
-
inhibition of glycolate-ferricyanide or glyoxylate-ferricyanide assay above 0.1 M
additional information
-
development of selective inhibitors of Hao2 from screening of a compound library, overview
-
additional information
-
treatment with 4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid or 4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid results in a significant reduction or attenuation of blood pressure in an established or developing model of hypertension, deoxycorticosterone acetate-treated rats
-
additional information
-
development of selective inhibitors of Hao2 from screening of a compound library, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
arsenate
-
increasing activity up to 0.1 M, inhibition of ferricyanide-linked assay above 0.1 M
phosphate
-
increasing activity up to 0.1 M, inhibition of ferricyanide-linked assay above 0.1 M
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
(s)-2-hydroxy-acid oxidase deficiency
Glycolate oxidase deficiency in a patient with congenital hyperinsulinism and unexplained hyperoxaluria.
Adenocarcinoma
Cellular mechanism of resistance of human colorectal adenocarcinoma cells against apoptosis-induction by Russell's Viper venom l-amino acid oxidase (Rusvinoxidase).
Adenocarcinoma
In vitro cytotoxicity of L-amino acid oxidase from the venom of Crotalus mitchellii pyrrhus.
Adenocarcinoma
The toxin BjussuLAAO-II induces oxidative stress and DNA damage, upregulates the inflammatory cytokine genes TNF and IL6, and downregulates the apoptotic-related genes BAX, BCL2 and RELA in human Caco-2 cells.
Breast Neoplasms
Apoptosis induction in human breast cancer (MCF-7) cells by a novel venom L-amino acid oxidase (Rusvinoxidase) is independent of its enzymatic activity and is accompanied by caspase-7 activation and reactive oxygen species production.
Carcinoma
Electrochemical immunosensor based on chitosan-gold nanoparticle/carbon nanotube as a ?platform and lactate oxidase as a ?label for detection of CA125 oncomarker?.
Colonic Neoplasms
Cytotoxic, Anti-Proliferative and Apoptosis Activity of l-Amino Acid Oxidase from Malaysian Cryptelytrops purpureomaculatus (CP-LAAO) Venom on Human Colon Cancer Cells.
Colonic Neoplasms
Cytotoxic, Antiproliferative and Apoptosis-inducing Activity of L-Amino Acid Oxidase from Malaysian Calloselasma rhodostoma on Human Colon Cancer Cells.
Colonic Neoplasms
L-amino acid oxidase from snake venom: Biotransformation and induction of apoptosis in human colon cancer cells.
Colorectal Neoplasms
Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah).
Colorectal Neoplasms
L-amino acid oxidase from snake venom: Biotransformation and induction of apoptosis in human colon cancer cells.
Congenital Hyperinsulinism
Glycolate oxidase deficiency in a patient with congenital hyperinsulinism and unexplained hyperoxaluria.
Dehydration
Nitrogen Metabolism in Adaptation of Photosynthesis to Water Stress in Rice Grown under Different Nitrogen Levels.
Edema, Cardiac
Aristolochic acid and its derivatives as inhibitors of snake venom L-amino acid oxidase.
Endometrial Neoplasms
Fraxetin inhibits the proliferation of RL95-2 cells through regulation of metabolism.
Fibrosarcoma
Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah).
Glioma
L-amino acid oxidase (LOX) modulation of melphalan activity against intracranial glioma.
Hyperoxaluria
Glycolate oxidase deficiency in a patient with congenital hyperinsulinism and unexplained hyperoxaluria.
Hyperoxaluria
Potential mechanisms of marked hyperoxaluria not due to primary hyperoxaluria I or II.
Hyperoxaluria, Primary
An Investigational RNAi Therapeutic Targeting Glycolate Oxidase Reduces Oxalate Production in Models of Primary Hyperoxaluria.
Hyperoxaluria, Primary
CRISPR/Cas9-mediated glycolate oxidase disruption is an efficacious and safe treatment for primary hyperoxaluria type I.
Hyperoxaluria, Primary
CRISPR/Cas9-mediated metabolic pathway reprogramming in a novel humanized rat model ameliorates primary hyperoxaluria type 1.
Hyperoxaluria, Primary
Dual Glycolate Oxidase/Lactate Dehydrogenase A Inhibitors for Primary Hyperoxaluria.
Hyperoxaluria, Primary
Glycolate Oxidase Is a Safe and Efficient Target for Substrate Reduction Therapy in a Mouse Model of Primary Hyperoxaluria Type I.
Hyperoxaluria, Primary
High resolution crystal structure of rat long chain hydroxy acid oxidase in complex with the inhibitor 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1, 2, 3-thiadiazole. Implications for inhibitor specificity and drug design.
Hyperoxaluria, Primary
High throughput cell-based assay for identification of glycolate oxidase inhibitors as a potential treatment for Primary Hyperoxaluria Type 1.
Hyperoxaluria, Primary
Inhibition of Glycolate Oxidase With Dicer-substrate siRNA Reduces Calcium Oxalate Deposition in a Mouse Model of Primary Hyperoxaluria Type 1.
Hyperoxaluria, Primary
Metabolism of (13)C5-hydroxyproline in mouse models of Primary Hyperoxaluria and its inhibition by RNAi therapeutics targeting liver glycolate oxidase and hydroxyproline dehydrogenase.
Hyperoxaluria, Primary
Metabolism of Oxalate in Humans: A Potential Role Kynurenine Aminotransferase/Glutamine Transaminase/Cysteine Conjugate Beta-lyase Plays in Hyperoxaluria.
Hyperoxaluria, Primary
Re: An Investigational RNAi Therapeutic Targeting Glycolate Oxidase Reduces Oxalate Production in Models of Primary Hyperoxaluria.
Hyperoxaluria, Primary
Re: CRISPR/Cas9-Mediated Glycolate Oxidase Disruption is an Efficacious and Safe Treatment for Primary Hyperoxaluria Type I.
Hyperoxaluria, Primary
Re: Glycolate Oxidase is a Safe and Efficient Target for Substrate Reduction Therapy in a Mouse Model of Primary Hyperoxaluria Type I.
Hyperoxaluria, Primary
Therapeutic RNA interference: A novel approach to the treatment of primary hyperoxaluria.
Infections
Expression profile of the fish immune enzyme l-amino acid oxidase (LAAO) after Streptococcus agalactiae infection in zebrafish (Danio rerio).
Infections
l-amino acid oxidase expression profile and biochemical responses of rabbitfish (Siganus oramin) after exposure to a high dose of Cryptocaryon irritans.
Kidney Calculi
Active site and loop 4 movements within human glycolate oxidase: implications for substrate specificity and drug design.
Kidney Calculi
Purification and characterization of recombinant human liver glycolate oxidase.
Kidney Failure, Chronic
High resolution crystal structure of rat long chain hydroxy acid oxidase in complex with the inhibitor 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1, 2, 3-thiadiazole. Implications for inhibitor specificity and drug design.
Leukemia
Cytotoxic proteins of Amanita virosa Secr. mushroom: purification, characteristics and action towards mammalian cells.
Melanoma
Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah).
Myotoxicity
Combined venomics, antivenomics and venom gland transcriptome analysis of the monocoled cobra (Naja kaouthia) from China.
Neoplasms
Antiproliferative Activity of King Cobra (Ophiophagus hannah) Venom l-Amino Acid Oxidase.
Neoplasms
CR-LAAO, an L-amino acid oxidase from Calloselasma rhodostoma venom, as a potential tool for developing novel immunotherapeutic strategies against cancer.
Neoplasms
Dual-Modal Therapeutic Role of the Lactate Oxidase-Embedded Hierarchical Porous Zeolitic Imidazolate Framework as a Nanocatalyst for Effective Tumor Suppression.
Neoplasms
Intra/Extracellular Lactic Acid Exhaustion for Synergistic Metabolic Therapy and Immunotherapy of Tumors.
Neoplasms
Isolation, characterization and screening of the in vitro cytotoxic activity of a novel L-amino acid oxidase (LAAOcdt) from Crotalus durissus terrificus venom on human cancer cell lines.
Neoplasms
King cobra (Ophiophagus hannah) venom L-amino acid oxidase induces apoptosis in PC-3 cells and suppresses PC-3 solid tumor growth in a tumor xenograft mouse model.
Neoplasms
l-Amino acid oxidase from Cerastes vipera snake venom: Isolation, characterization and biological effects on bacteria and tumor cell lines.
Neoplasms
L-amino acid oxidase from snake venom: Biotransformation and induction of apoptosis in human colon cancer cells.
Neoplasms
l-Amino acid oxidase isolated from Calloselasma rhodostoma snake venom induces cytotoxicity and apoptosis in JAK2V617F-positive cell lines.
Neoplasms
Openwork@Dendritic Mesoporous Silica Nanoparticles for Lactate Depletion and Tumor Microenvironment Regulation.
Neoplasms
Oxidoreductase activities in normal rat liver, tumor-bearing rat liver, and hepatoma HC-252.
Neoplasms
Peroxisome inspired hybrid enzyme nanogels for chemodynamic and photodynamic therapy.
Neoplasms
Repolarization of M2 to M1 macrophages triggered by lactate oxidase released from methylcellulose hydrogel.
Neoplasms
Targeting Tumor Microenvironment by Bioreduction-Activated Nanoparticles for Light-Triggered Virotherapy.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
L-amino acid oxidase isolated from Micrurus mipartitus snake venom (MipLAAO) specifically induces apoptosis in acute lymphoblastic leukemia cells mostly via oxidative stress-dependent signaling mechanism.
Precursor T-Cell Lymphoblastic Leukemia-Lymphoma
L-amino acid oxidase isolated from Micrurus mipartitus snake venom (MipLAAO) specifically induces apoptosis in acute lymphoblastic leukemia cells mostly via oxidative stress-dependent signaling mechanism.
Pulmonary Edema
Aristolochic acid and its derivatives as inhibitors of snake venom L-amino acid oxidase.
Stomach Neoplasms
Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah).
Thrombocytopenia
Comparative proteomes, immunoreactivities and neutralization of procoagulant activities of Calloselasma rhodostoma (Malayan pit viper) venoms from four regions in Southeast Asia.
Unconsciousness
Danger in the Canopy. Comparative Proteomics and Bioactivities of the Venoms of the South American Palm Pit Viper Bothrops bilineatus Subspecies bilineatus and smaragdinus and Antivenomics of B. b. bilineatus (Rondônia) Venom against the Brazilian Pentabothropic Antivenom.
Urolithiasis
Experimental urolithiasis : Part II--a comparative kinetic study of glyoxalase I, glycolate oxidase, alkaline phosphatase & lactate dehydrogenase in the normal rat kidney & bladder & its alterations in urolithiasis.
Uterine Cervical Neoplasms
ACTX-8, a cytotoxic L-amino acid oxidase isolated from Agkistrodon acutus snake venom, induces apoptosis in Hela cervical cancer cells.
Virus Diseases
Barley Stripe Mosaic Virus ?b Interacts with Glycolate Oxidase and Inhibits Peroxisomal ROS Production to Facilitate Virus Infection.
Vitamin B 6 Deficiency
Vitamin B6 deficiency as related to oxalate-synthesizing enzymes in growing rats.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
25.5
(S)-lactate
-
25°C, mutant enzyme E160G/V198I/G36S/T103S/A232S/F277Y
47.6
(S)-lactate
-
35°C, mutant enzyme E160G/V198I/G36S/T103S/A232S/F277Y
0.24
glycolate
pH 7.5, temperature not specified in the publication
additional information
additional information
-
mesophyll isoform shows higher affinity for glycolate than bundle sheath isoform
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
stopped-flow, steady-state, and presteady-state kinetics at different pH values, pH profiles, detailed overview
-
additional information
additional information
-
stopped-flow, steady-state, and presteady-state kinetics at different pH values, pH profiles, detailed overview
-
additional information
additional information
-
reduction rate constants and dissociation constants for reaction of lactate oxidases with alpha-1H- and alpha-2H-para-substituted mandelates
-
additional information
additional information
-
Michaelis-Mentin kinetics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
glycolate
pH 7.5, temperature not specified in the publication
additional information
additional information
a second-order rate constant for the capture of glycolate (kcat/Kglycolate) of 68300 M/s, and a second-order rate constant for reaction of the reduced flavin with oxygen (kcat/Koxygen) of 24500 Ms
-
additional information
additional information
-
a second-order rate constant for the capture of glycolate (kcat/Kglycolate) of 68300 M/s, and a second-order rate constant for reaction of the reduced flavin with oxygen (kcat/Koxygen) of 24500 Ms
-
additional information
additional information
-
reduction rate constants and dissociation constants for reaction of lactate oxidases with alpha-1H- and alpha-2H-para-substituted mandelates
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.25
glycolate
pH 7.5, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
straight-chain monocarboxylic acids are non-competitive inhibitors with either glycolate or glyoxylate as substrates, dicarboxylic acids are competitive inhibitors with glycolate as substrate, but non-competitive inhibitors for glyoxylate as substrate
-
494
acetate
-
decreasing values as the number of carbons in the alkyl side chain increases from 1 to 2 and to 5
0.44
oxalate
-
competitive, glycolate oxidation, non-competitive for glyoxylate oxidation
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0007 - 0.0108
3-benzyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
0.0003 - 0.0054
3-ethyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
0.0003 - 0.00634
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
0.002 - 0.0113
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
0.0004 - 0.0083
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
0.0011 - 0.0051
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
0.0091
4-(biphenyl-3-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0002 - 0.0186
4-[(4'-carbamoylbiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
0.0011 - 0.0032
4-[(4'-carboxybiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
0.0004 - 0.01125
4-[(4'-fluorobiphenyl-4-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
0.0009 - 0.0095
4-[2-(4'-fluorobiphenyl-3-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
0.0009 - 0.0054
4-[2-(4'-fluorobiphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
0.00091
4-[2-(biphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0004 - 0.0022
4-[[4'-(2-amino-2-oxoethyl)biphenyl-3-yl]methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
0.0008 - 0.0042
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
0.0005 - 0.0021
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(propan-2-yl)-1H-pyrazole-5-carboxylic acid
0.0011 - 0.0018
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-phenyl-1H-pyrazole-5-carboxylic acid
0.0007
3-benzyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0108
3-benzyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0012
3-ethoxy-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0012
3-ethoxy-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0003
3-ethyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0054
3-ethyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0095
3-methyl-4-(2-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0107
3-methyl-4-(2-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00427
3-methyl-4-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
427
3-methyl-4-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0006
3-methyl-4-(3-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0124
3-methyl-4-(3-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0005
3-methyl-4-(4-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0104
3-methyl-4-(4-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0002
3-methyl-4-(naphthalen-1-ylmethyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0226
3-methyl-4-(naphthalen-1-ylmethyl)-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0011
3-methyl-4-(naphthalen-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00812
3-methyl-4-(naphthalen-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0017
3-methyl-4-(quinolin-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0022
3-methyl-4-(quinolin-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0007
3-methyl-4-[2-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0023
3-methyl-4-[2-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0013
3-methyl-4-[2-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0134
3-methyl-4-[2-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0004
3-methyl-4-[3-(pyridin-3-yl)benzyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0315
3-methyl-4-[3-(pyridin-3-yl)benzyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0003
3-methyl-4-[3-(pyridin-4-yl)benzyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0135
3-methyl-4-[3-(pyridin-4-yl)benzyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0003
3-methyl-4-[3-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00523
3-methyl-4-[3-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0013
3-methyl-4-[4-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0073
3-methyl-4-[4-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00912
3-methyl-4-[4-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0357
3-methyl-4-[4-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0003
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00634
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.002
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0113
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0004
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0083
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0011
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0051
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0267
4-(1-benzofuran-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.048
4-(1-benzofuran-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0003
4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0083
4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0009
4-(3-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0088
4-(3-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.003
4-(3-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0076
4-(3-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0005
4-(3-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0062
4-(3-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0002
4-(3-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00113
4-(3-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00095
4-(4'-fluorobiphenyl-3-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0358
4-(4'-fluorobiphenyl-3-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0137
4-(4'-fluorobiphenyl-4-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0196
4-(4'-fluorobiphenyl-4-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0008
4-(4-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
11
4-(4-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0032
4-(4-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0407
4-(4-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0006
4-(4-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0339
4-(4-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0007
4-(4-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00714
4-(4-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00135
4-(4-fluorophenyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0031
4-(4-fluorophenyl)-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0009
4-[(2'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0052
4-[(2'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0005
4-[(3'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0205
4-[(3'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0002
4-[(4'-carbamoylbiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0186
4-[(4'-carbamoylbiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0011
4-[(4'-carboxybiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0032
4-[(4'-carboxybiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0003
4-[(4'-cyanobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0135
4-[(4'-cyanobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0116
4-[(4'-fluorobiphenyl-2-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0217
4-[(4'-fluorobiphenyl-2-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0003
4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0166
4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0004
4-[(4'-fluorobiphenyl-4-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.01125
4-[(4'-fluorobiphenyl-4-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0009
4-[2-(4'-fluorobiphenyl-3-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0095
4-[2-(4'-fluorobiphenyl-3-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0009
4-[2-(4'-fluorobiphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0054
4-[2-(4'-fluorobiphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0052
4-[2-(4-fluorophenyl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0318
4-[2-(4-fluorophenyl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0004
4-[[4'-(2-amino-2-oxoethyl)biphenyl-3-yl]methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0022
4-[[4'-(2-amino-2-oxoethyl)biphenyl-3-yl]methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0008
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0042
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0005
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(propan-2-yl)-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0021
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(propan-2-yl)-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0011
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-phenyl-1H-pyrazole-5-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0018
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-phenyl-1H-pyrazole-5-carboxylic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.45
0.55
20
-
commercial preparation, pH not specified in the publication, temperature not specified in the publication
28.07
type 1 enzyme expressed in Escherichia coli BL21Star, 10 mM potassium phophate, pH 6,5, 0.01 mM flavin adenine nucleotide, 37°C, 0.02% 2,2-azinobis (3-ethylbenzthiazolinesulfonic acid), 10 mM L-(+)-lactate, 0.5 U horseradish peroxidase (peroxidase-coupled spectrophotometric assay)
41
-
commercial preparation, pH 7.0, temperature not specified in the publication
45.76
type 2 enzyme expressed in Escherichia coli BL21Star, 10 mM potassium phophate, pH 6.5, 0.01 mM flavin adenine nucleotide, 37°C, 0.02% 2,2-azinobis (3-ethylbenzthiazolinesulfonic acid), 10 mM L-(+)-lactate, 0.5 U horseradish peroxidase (peroxidase-coupled spectrophotometric assay)
72
-
commercial preparation, pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
decrease of enzyme activity upon oxidative stress induced by glutathione depletion or postischemic perfusion
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
8.8
8.8
-
0.1 M Tris buffer, compromise between optimal lactate oxidase pH 7.5 and optimal pH of 9.5 for peroxidase from Arthromyces ramosus in the combined biosensor system
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
pH profiles, the enzyme shows a ping-pong bi-bi kinetic mechanism between pH 6.0 and 10.0, overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
correlation of enzyme activity with content of beta-N-oxalyl-L-alpha,beta-diaminopropionic acid under high light treatment
-
-
brenda
-
287560, 389680, 389685, 389686, 389687, 389688, 389689, 389690, 389691, 389692, 389693, 389694, 389698, 389700, 389703
-
-
brenda
type 2 lactate oxidase isolated from Strptococcus iniae; major pathogen of farmed fish, type 2 is an isolate from diseased barramundi (Lates calcarifer) in Northern Territory, Australia
UniProt
brenda
activities of both lactarte oxidase and pyruvate oxidase in wild-type cultures are detectable even in the early exponential phase of growth and attain the highest levels in the early stationary phase
-
-
brenda
-
-
-
brenda
authors suggest a different annotation for the lctO gene with LctO translation starting at Met-18, encoding a protein of 366 amino acids
UniProt
brenda
authors suggest a different annotation for the lctO gene with LctO translation starting at Met-18, encoding a protein of 366 amino acids
UniProt
brenda
type 2 lactate oxidase isolated from Strptococcus iniae; major pathogen of farmed fish, type 2 is an isolate from diseased barramundi (Lates calcarifer) in Northern Territory, Australia
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
germinated seed, expression level is similar to ubiquitin
brenda
additional information
HAO2 mRNA levels are strongly downregulated in two distinct series of human HCCs, when compared to both normal and cirrhotic peritumoral liver, overview
brenda
Hao2 is highly significantly downregulated in 12/12 HCCs developed by the CMD protocol and in 16/16 HCCs generated by chronic DENA treatment
brenda
-
Hao2 is highly significantly downregulated in 12/12 HCCs developed by the CMD protocol and in 16/16 HCCs generated by chronic DENA treatment
-
brenda
predominant expression, abundantly expressed in leaves and leaf sheaths
brenda
leaf and sheath, predominant expression
brenda
additional information
-
one isoform is located in bundle sheath cells, the second isozyme has dual location, and the third one is located in mesophyll cells
brenda
additional information
-
hepatic or leaf glycolate oxidases oxidize best glycolate and alpha-hydroxyisocaproate, that from kidney oxidizes only long-chain alpha-hydroxy acids
brenda
additional information
-
Kidney enzyme oxidizes only long-chain alpha-hydroxy acids. The liver enzyme also oxidizes L-amino acids
brenda
additional information
-
influence of growth conditions on enzyme expression, overview
brenda
additional information
plant
-
hepatic or leaf glycolate oxidases oxidize best glycolate and alpha-hydroxyisocaproate, that from kidney oxidizes only long-chain alpha-hydroxy acids
brenda
additional information
-
hepatic or leaf glycolate oxidases oxidize best glycolate and alpha-hydroxyisocaproate, that from kidney oxidizes only long-chain alpha-hydroxy acids
brenda
additional information
expression is negligible in embryos and the endosperm of germinated seeds
brenda
additional information
expression is negligible in embryos and the endosperm of germinated seeds
brenda
additional information
-
expression is negligible in embryos and the endosperm of germinated seeds
brenda
additional information
-
influence of growth conditions on enzyme expression, overview
brenda
additional information
-
the enzyme is expressed throughout the growth phase, and expression of the lox gene increases by about 2.5fold when cells enter the stationary phase
brenda
additional information
-
influence of growth conditions on enzyme expression, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
subcellular localization analysis, no enzyme activity in cytosol, mitochondrial membrane, or mitochondrial matrix, overview
-
brenda
a C-terminal fluorescent fusion localizes to the cytosol in tobacco protoplasts
brenda
-
preparation of heavy and light mitochondria, 2 distinct molecular forms
brenda
-
confocal immunofluorescence microscopy reveals that capsid protein P8 is colocalized with GOX in peroxisomes
brenda
the enzyme contains a peroxisomal targeting signale -ARL
brenda
an N-terminal fluorescent fusion protein colocalizes with an peroxisomal marker in tobacco protoplasts
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the enzyme belongs to the family of L-2-hydroxy acid oxidases
evolution
the enzyme belongs to the family of L-2-hydroxy acid oxidases
evolution
enzyme glycolate oxidase, GOX, belongs to the gene family of (L)-2-hydroxyacid-oxidases ((L)-2-HAOX). In addition to GOX, plants possess (L)-2-HAOX proteins with different specificities for medium- and long-chain hydroxyacids (lHAOX), likely involved in fatty acid and protein catabolism. Vertebrates possess lHAOX proteins acting on similar substrates as plant lHAOX. The existence of GOX and lHAOX subfamilies in both plants and animals is not due to shared ancestry but is the result of convergent evolution in the two most complex eukaryotic lineages. Duplication and diversification occurred independently at the base of deuterostomia and at the base of vascular plants. The biological role of plantae (L)-2-HAOX in photorespiration evolved by coopting an existing peroxisomal protein, targeting sequences and predicted substrate specificities, phylogenetic analysis and tree, hypothesis for the evolution of the (L)-2-HAOX gene family, overview. Convergent evolution in vascular plants and deuterostomia
evolution
enzyme glycolate oxidase, GOX, belongs to the gene family of (L)-2-hydroxyacid-oxidases ((L)-2-HAOX). The encoding gene is thought to have originated from endosymbiotic gene transfer between the eukaryotic host and the cyanobacterial endosymbiont at the base of plantae. Animals also possess GOX activities. Plant and animal GOX belong to the gene family of (L)-2-hydroxyacid-oxidases ((L)-2-HAOX). In addition to GOX, plants possess (L)-2-HAOX proteins with different specificities for medium- and long-chain hydroxyacids (lHAOX), likely involved in fatty acid and protein catabolism. The biological role of plantae (L)-2-HAOX in photorespiration evolved by coopting an existing peroxisomal protein, targeting sequences and predicted substrate specificities, phylogenetic analysis and tree, hypothesis for the evolution of the (L)-2-HAOX gene family, overview
evolution
-
the enzyme belongs to the family of L-2-hydroxy acid oxidases
-
malfunction
the enzyme is involved in primary hyperoxaluria, a genetic disorder where overproduction of oxalate results in the formation of kidney stones
malfunction
evaluation of the potential of siRNAs targeting the synthesis of liver glycolate oxidase or hydroxyproline dehydrogenase formulated in lipid nanoparticles, to reduce urinary oxalate excretion in Agxt KO mice. The siRNA targeting glycolate oxidase blocks a downstream step and prevents the synthesis of glyoxylate from glycolate in the liver. The ability of such siRNAs to reduce urinary oxalate in the mouse model suggests that this approach is promising for the treatment of primary hyperoxalurias, PH, particularly PH type I, in humans
malfunction
an alternative approach to prevent glyoxylate production in subjects with primary hyperoxaluria type 1 (PH1) is using Dicer-substrate small interfering RNAs (DsiRNAs) targeting hydroxyacid oxidase 1 (HAO1) mRNA, which encodes glycolate oxidase (GO), to reduce the hepatic conversion of glycolate to glyoxylate. This approach efficiently reduces GO mRNA and protein in the livers of mice. Reduction of hepatic GO leads to normalization of urine oxalate levels and reduces CaOx deposition in a preclinical mouse model of PH1. Hao1-/- mice show elevated levels of urinary glycolate without renal damage or other phenotypic consequences
malfunction
-
an alternative approach to prevent glyoxylate production in subjects with primary hyperoxaluria type 1 (PH1) is using Dicer-substrate small interfering RNAs (DsiRNAs) targeting hydroxyacid oxidase 1 (HAO1) mRNA, which encodes glycolate oxidase (GO), to reduce the hepatic conversion of glycolate to glyoxylate. This approach efficiently reduces GO mRNA and protein in the livers of mice. Reduction of hepatic GO leads to normalization of urine oxalate levels and reduces CaOx deposition in a preclinical mouse model of PH1. Hao1-/- mice show elevated levels of urinary glycolate without renal damage or other phenotypic consequences
-
malfunction
-
evaluation of the potential of siRNAs targeting the synthesis of liver glycolate oxidase or hydroxyproline dehydrogenase formulated in lipid nanoparticles, to reduce urinary oxalate excretion in Agxt KO mice. The siRNA targeting glycolate oxidase blocks a downstream step and prevents the synthesis of glyoxylate from glycolate in the liver. The ability of such siRNAs to reduce urinary oxalate in the mouse model suggests that this approach is promising for the treatment of primary hyperoxalurias, PH, particularly PH type I, in humans
-
metabolism
the enzyme is involved in the glyoxylate metabolism, overview
metabolism
-
the enzyme is involved in the metabolism of glycolate, glycolate oxidase is a key enzyme involved in C3 photorespiration metabolic pathway, the process where plants lose up to half of assimilated carbon
metabolism
-
inactivation of gene pox encoding pyruvate oxidase causes a dramatic reduction in H2O2 production from lactate, suggesting a synergistic action of the two oxidases in converting lactate into H2O2. The pox mutant of Streptomyces oligofermentans fails to inhibit Streptomyces mutans even though lox is active
physiological function
a positive and linear correlation exists between GLO activities and the net photosynthetic rates, PN, and photoinhibition subsequently occurrs once PN reduction surpasses 60%, indicating GLO can exert a strong regulation over photosynthesis. Isocitrate lyase and malate synthase, two key enzymes in the glyoxylate cycle, are highly up-regulated under GLO deficiency
physiological function
-
the enzyme performs an essential step in the operation of the oxidative photorespiratory cycle accompanying photosynthetic CO2 assimilation in C3 plants
physiological function
-
role in C3 and C4 plants and associated regulation mechanisms
physiological function
-
role in C3 and C4 plants and associated regulation mechanisms
physiological function
-
H2O2 production, especially lactate oxidase, allows Streptomyces oligofermentans to out-compete Streptomyces mutans in oral commensals, the enzyme mainly contributes to H2O2 production in stationary phase. But lactate oxidase requires cofunction of pyruvate oxidase for successfully inhibiting Streptomyces mutans
physiological function
-
pharmacological role of the enzyme in the management of blood pressure
physiological function
L-2-hydroxy acid oxidases are flavin mononucleotide-dependent peroxisomal enzymes, responsible for the oxidation of L-2-hydroxy acids to ketoacids, resulting in the formation of hydrogen peroxide. Oncosuppressive role of HAO2 in hepatocarcinogenesis
physiological function
L-2-hydroxy acid oxidases are flavin mononucleotide-dependent peroxisomal enzymes, responsible for the oxidation of L-2-hydroxy acids to ketoacids, resulting in the formation of hydrogen peroxide. Oncosuppressive role of HAO2 in hepatocarcinogenesis
physiological function
L-2-hydroxy acid oxidases are flavin mononucleotide-dependent peroxisomal enzymes, responsible for the oxidation of L-2-hydroxy acids to ketoacids, resulting in the formation of hydrogen peroxide. Oncosuppressive role of HAO2 in hepatocarcinogenesis
physiological function
glycolate oxidase (GOX) is a crucial enzyme of plant photorespiration
physiological function
-
inoculation of plants with Pseudomonas syringae increases photorespiration rate and expression of glycolate oxidase (GOX2), serine glyoxylate aminotransferase (SGT) and serine hydroxyl methyltransferase (SHMT1). Silencing of GOX2, SGT or SHMT1 genes in tomato decreases photorespiration but increases susceptibility to Pseudomonas syringae, whereas transient overexpression of GOX2, SGT or SHMT1 in tobacco increases basal defence. Salicylic acid signalling is involved in GOX2-mediated, SGT-mediated and SHMT1-mediated defence. H2O2 pretreatment remarkably alleviates the GOX2 silencing-induced depression in basal defence and salicylic acid signalling
physiological function
barley stripe mosaic virus BSMV gammab protein inhibits GOX enzymatic activity, peroxisomal free radicals, and ROS bursts under BSMV infection. GOX interacts with virus protein BSMV gammab. Deletion of gammab from BSMV abolishes inhibition of GOX activity in vivo, and GOX enzymatic activity is reduced in gammab transiently expressing cells. Presence of a GST-gammab construct greatly reduces recombinant GOX enzymatic activity. GOX mRNA decreases during BSMV infection
physiological function
-
sixteen GOX genes are found in Nicotiana benthamiana genome. They consist of GOX and HAOX groups. All but two GOX proteins contain an alpha_hydroxyacid_oxid_FMN domain with extra 433-52 amino acids compared to that of FMN-dependent alpha-hydroxyacid oxidizing enzymes. Silencing of three GOX family genes NbHAOX8, NbGOX1 and NbGOX4 differently affects resistance to various pathogens including Tobacco rattle virus, Xanthomonas oryzae pv. oryzae (Xoo) and Sclerotinia sclerotiorum. Effect of these genes on resistance to Xoo is well correlated with that on Xoo-responsive H2O2 accumulation. Silencing of these genes enhances PAMP peptide flg22-triggered immunity
physiological function
-
L-2-hydroxy acid oxidases are flavin mononucleotide-dependent peroxisomal enzymes, responsible for the oxidation of L-2-hydroxy acids to ketoacids, resulting in the formation of hydrogen peroxide. Oncosuppressive role of HAO2 in hepatocarcinogenesis
-
physiological function
-
L-2-hydroxy acid oxidases are flavin mononucleotide-dependent peroxisomal enzymes, responsible for the oxidation of L-2-hydroxy acids to ketoacids, resulting in the formation of hydrogen peroxide. Oncosuppressive role of HAO2 in hepatocarcinogenesis
-
additional information
the key residue Tyr129 in the active site of LCHAO does affect L-lactate binding to LCHAO but plays an important role on the catalytic reaction process through an H-bond interaction. Generation of a structural model of LCHAO-FMN-lactate. The active site informed by residues Phe23, Tyr129, Asp157, Arg164, Lys223, His247, and Arg250
additional information
structure homology modeling of Arabidopsis thaliana lHAOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana lHAOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana lHAOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana lHAOX2 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana lHAOX2 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana lHAOX2 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana GOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana GOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
additional information
structure homology modeling of Arabidopsis thaliana GOX1 based on the crystal structure of Spinacia oleracea GOX, PDB ID 1GOX
Show AA Sequence and Transmembrane Helices (5477 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
150000
-
isoenzymes A and B, gel filtration, sedimentation equilibrium analysis, self-association at low protein concentrations
160000
37000
39000
41290
-
determined by mass spectrometry. After tag-removal two close bands appear on SDS-PAGE one at 45.287 kDa and one at 41.288 kDa
44000
44040
calculated, 407 amino acids, 920 bp, 51 bp repeat sequence compared to type 1 enzyme
45290
-
determined by mass spectrometry. After tag-removal two close bands appear on SDS-PAGE one at 45.287 kDa and one at 41.288 kDa
50000
-
8 * 50000, transmission electron microscopy analysis and SDS-PAGE
160000
small-angle X-ray scattering, gel filtration and structural analysis
37000
-
x * 44000, bundle sheath cell isozyme, SDS-PAGE, x * 37000, mesophyll cell isozyme, SDS-PAGE
44000
-
x * 44000, bundle sheath cell isozyme, SDS-PAGE, x * 37000, mesophyll cell isozyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
octamer
tetramer
additional information
?
-
x * 44000, bundle sheath cell isozyme, SDS-PAGE, x * 37000, mesophyll cell isozyme, SDS-PAGE
?
x * 39900, recombinant enzyme without tag, SDS-PAGE
?
x * 40100, recombinant enzyme without tag, SDS-PAGE
octamer
-
8 * 50000, transmission electron microscopy analysis and SDS-PAGE
additional information
-
gene glcD encodes the D-subunit of the glycolate oxidase
additional information
structure analysis, modelling, the enzyme shows the same beta8alpha8 TIM barrel structure as other structurally characterized family members of the FMN-dependent enzyme family
additional information
-
molecular modeling studies using the rat Hao2 crystal structure, PDB ID 1TB3, overview
additional information
-
gene glcD encodes the D-subunit of the glycolate oxidase
additional information
-
gene glcD encodes the D-subunit of the glycolate oxidase
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3.0 A resolution, octamer with non-crystallographic two- and four-fold axes
-
hanging-drop or sitting-drop vapour diffusion method, 2.44 A resolution, large diffracting crystals of LOXR181M are obtained. LOX-R181M crystals belong to the tetragonal space group I422, with unit-cell parameters a = b = 192.632 A, c= 200.263 A, alpha = beta = gamma =90°. There are four monomers in the asymmetric unit
-
resolution to 1.9 A. One pyruvate molecule is bound to the active site and located near N5 position of FMN for subunits, A, B, and D in the asymmetric unit. The pyruvate molecule is stabilized by the interaction of its carboxylate group with the side-chain atoms of Tyr40, Arg181, His265, and Arg268, and of its keto-oxygen atom with the side-chain atoms of Tyr146, Tyr215, and His265
-
sitting-drop vapor diffusion technique. Crystal structure of wild-type enzyme at 2.1 A resolution. Space group I422 of unit-cell parameters a = b = 191.096 A, c = 194.497 A and alpha = beta = gamma = 90° with four monomers per asymmetric unit
-
sitting-drop vapour-diffusion method, determination of structure at 2.1 A resolution
-
unbound enzyme and in complex with D-lactate, both at pH 4.5. In the complex structure, the D-lactate resides in the substrate-binding site, but an active site base, His265, flips far away from the D-lactate, as compared with its conformation in the unbound state at pH 8.0. The flip of His265 triggers a large structural rearrangement, creating a new hydrogen bonding network between His265-Asp174-Lys221 and, furthermore, brings molecular oxygen in between D-lactate and His265. In the mechanism of the subsequent oxidative half-reaction, His265 flips back, pushing molecular oxygen into the substrate-binding site as the second substrate, and the reverse reaction takes place to produce hydrogen peroxide
-
structures of recombinant GO complexed with sulfate, glyoxylate, and 4-carboxy-5-dodecylsulfanyl-1,2,3-triazole (CDST), determined by X-ray crystallography are reported. A loop region (loop 4), is completely visible when the GO active site contains a small ligand. Lack of electron density for this loop in the GOCDST complex, mimicking a large substrate, indicates that a disordered to ordered transition occurs with substrate binding. Conformational flexibility of Trp110 is responsible for enabling GO to react with R-hydroxy acids. Movement of Trp110 disrupts a hydrogen-bonding network between Trp110, Leu191, Tyr134, and Tyr208. This loss indicates that active site movements are directly linked to changes in the conformation of loop 4
apo-GOX structure and its complex structure with cofactor FMN. The binding of FMN induces a pronounced conformational change of the GOX tetramer. A conserved pH sensor found among different species might directly regulate the binding of FMN and the enzyme activity
study of the nanomechanical properties of lactate oxidase monolayer immobilized on gold substrate by atomic force microscopy. The data fit by the Hertz model for a conical indenter, an average value of Young's modulus for the protein layer is in the 0.5-0.8 GPa range
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analysis of the crystal structure of enzyme LCHAO in complex with cofactor FMN and inhibitor 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1,2,3-thiadiazole (CCPST) at 1.3 A resolution
sitting drop vapor diffusion method, 0.005 ml of protein solution containing 10 mg/ml protein in 0.1 M Tris, pH 7.5, mixed with the same volume of reservoir solution containing 0.4 M sodium acetate and 0.2 M sodium citrate, pH 6.5, equilibration at 4°C, soaking of crystals in 25% glycerol-containing reservoir solution, X-ray diffraction structure determination and analysis at 2.3 A resolution
ammonium sulfate precipitation, 2.6 A resolution of a two subunit apoenzyme
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A95G
E160G/V198I
-
the half-life of the mutant lactate oxidase at 70°C is about 18times that of the wild-type enzyme. Km-value for (S)-lactate at 25°C is 46fold higher than wild-type value, Km-value for (S)-lactate at 25°C is 59fold higher than wild-type value
E160G/V198I/G36S/T103S/A232S/F277Y
-
the half-life of the mutant lactate oxidase at 70°C is about 2 times that of E160G/V198I mutant and about 36 times that of the wild-type enzyme. Km-value for (S)-lactate at 25°C is 48fold higher than wild-type value, Km-value for (S)-lactate at 25°C is 55fold higher than wild-type value. Mutant is obtained by direct evolution
Y129F
site-directed mutagenesis of the key active site residue, the mutant enzymes shows highly reduced kcat but unaltered Km value compared to wild-type enzyme, modeling of the hydride transfer of mutant enzyme with bound FMN and lactate, the missing H-bond changes the mechanism of the LCHAO Y129F mutant catalyzed oxidation reaction
additional information
A95G
-
much enhanced oxidase activity with longer chain L-alpha-hydroxyacids such as alpha-hydroxy-n-butyric acid, alpha-hydroxy-n-valeric acid and L-mandelic acid
A95G
-
enhanced activity with bulky substrates, increase in the reduction rate constants with substrates having a bulky alpha-substituent such as mandelate, when compared with wild-type enzyme
additional information
Arabidopsis thaliana plants overexpressing glycolate oxidase in chloroplasts accumulates both hydrogen peroxide and glyoxylate, enzyme-overexpressing plants show retarded development, yellowish rosettes, and impaired photosynthetic performance. The plants develop oxidative stress lesions under photorespiratory conditions but grow like wild-type plants under nonphotorespiratory conditions, phenotype, overview
additional information
enzyme knockout by specific siRNA targeting the liver enzyme glycolate oxidase in wild-type leads to greatly decreased GO activity, 20fold increased urinary excretion of glycolate, and more than 2fold increased urinary oxalate excretion compared to controls. Treatment of mutant Agxt KO mice, that are deficient in liver alanine:glyoxylate aminotransferase, leads to significantly decreased urinary oxalate excretion, but substantially increased urinary glycolate excretion
additional information
-
enzyme knockout by specific siRNA targeting the liver enzyme glycolate oxidase in wild-type leads to greatly decreased GO activity, 20fold increased urinary excretion of glycolate, and more than 2fold increased urinary oxalate excretion compared to controls. Treatment of mutant Agxt KO mice, that are deficient in liver alanine:glyoxylate aminotransferase, leads to significantly decreased urinary oxalate excretion, but substantially increased urinary glycolate excretion
additional information
Rattus norvegicus hepatocellular carcinoma cells are transduced by a HAO2 encoding lentiviral vector and grafted in mice
additional information
enzyme knockout by Dicer-substrate small interfering RNAs (DsiRNAs) targeting hydroxyacid oxidase 1 (HAO1) mRNA, relationship of Hao1 mRNA and glycolate oxidase protein knockdown to oxalate reduction, overview
additional information
-
enzyme knockout by Dicer-substrate small interfering RNAs (DsiRNAs) targeting hydroxyacid oxidase 1 (HAO1) mRNA, relationship of Hao1 mRNA and glycolate oxidase protein knockdown to oxalate reduction, overview
additional information
-
Rattus norvegicus hepatocellular carcinoma cells are transduced by a HAO2 encoding lentiviral vector and grafted in mice
-
additional information
-
enzyme knockout by Dicer-substrate small interfering RNAs (DsiRNAs) targeting hydroxyacid oxidase 1 (HAO1) mRNA, relationship of Hao1 mRNA and glycolate oxidase protein knockdown to oxalate reduction, overview
-
additional information
-
enzyme knockout by specific siRNA targeting the liver enzyme glycolate oxidase in wild-type leads to greatly decreased GO activity, 20fold increased urinary excretion of glycolate, and more than 2fold increased urinary oxalate excretion compared to controls. Treatment of mutant Agxt KO mice, that are deficient in liver alanine:glyoxylate aminotransferase, leads to significantly decreased urinary oxalate excretion, but substantially increased urinary glycolate excretion
-
additional information
-
yeast two-hybrid and co-immunoprecipitation assays indicate that capsid protein P8, an outer capsid protein of Rice dwarf phytoreovirus (RDV), interacts with rice glycolate oxidase (GOX)
additional information
-
co-expression of GOX with capsid protein P8 targets capsid protein P8 into peroxisomes: time course analysis demonstrates that the localization of capsid protein P8 in peroxisomes of Spodoptera frugiperda cells, co-expressing capsid protein P8 and GOX, changes from diffuse to discrete, punctuate inclusions during expression from 24 to 48 h post inoculation
additional information
phenotypes of GLO-suppressed plants under air and high CO2, overview. The plants with 30%, 60%, and 90% reduced GLO activities accumulate 40, 60, and 130fold, respectively, more glycolate than the wild-type
additional information
-
phenotypes of GLO-suppressed plants under air and high CO2, overview. The plants with 30%, 60%, and 90% reduced GLO activities accumulate 40, 60, and 130fold, respectively, more glycolate than the wild-type
additional information
-
construction and evaluation of a biosensor of chiral, biocompatible, conducting material comprising collagen I, silica gel and ferrocene involving glucose oxidase/lactate oxidase enzymes. Preparation of the ferrocene/collagen or ferrocene/collagen/silica modified electrodes. The material modifies and inverts the chiral selectivity of D-glucose oxidase and L-lactate oxidase in collagen incorporated in tetramethoxysilane, overview
additional information
-
immobilization of the enzyme from water-organic solvent mixture on biosensor membranes, most active enzyme containing membranes are obtained using triethoxysiloxanes: gamma-aminopropyl-,vinyl-, or phenyl-triethoxysiloxane, method optimization and evaluation, overview. Lactate oxidase remains with more than 60% of it is initial activity after exposing to water-isopropanol mixtures with over 90% v/v content of organic solvent
additional information
-
imobilization of the enzyme on gold electrodes, determination of lactate oxidase patterns with gold substrates, in terms of homogeneity, compactness and stability, overview. LOx is directly stamped to a bare gold surface, LOx is previously covalently bonded to a thiolated molecule, dithiodipropionic acid di-N-succinimidyl ester, and this conjugate is transferred from an elastomeric stamp to a bare gold substrate, formation of a LOx/DTSP micropattern on a bare gold surface, which is followed by exposure to a solution containing hexadecylmercaptane
additional information
Rattus norvegicus hepatocellular carcinoma cells are transduced by a HAO2 encoding lentiviral vector and grafted in mice
additional information
-
Rattus norvegicus hepatocellular carcinoma cells are transduced by a HAO2 encoding lentiviral vector and grafted in mice
-
additional information
-
in an enzyme disruption mutant, the highest concentration of H2O2 attained in the medium is found to be approximately 1 mM, about one-fifth the level for the parental strain. Although cell growth continuous until glucose in the medium becomes undetectable even in the absence of added catalase, the maximum cell mass attained is considerably higher in the presence of catalase than in its absence. The maximum cell mass achieved in the presence of added catalase is reproducibly lower by 0.2 to 0.3 turbidity units than that of the parent
additional information
-
in an enzyme disruption mutant, the highest concentration of H2O2 attained in the medium is found to be approximately 1 mM, about one-fifth the level for the parental strain. Although cell growth continuous until glucose in the medium becomes undetectable even in the absence of added catalase, the maximum cell mass attained is considerably higher in the presence of catalase than in its absence. The maximum cell mass achieved in the presence of added catalase is reproducibly lower by 0.2 to 0.3 turbidity units than that of the parent
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
-
20 min, 25°C, more than 80% residual activity, recombinant protein
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
70
50
-
20 min, more than 40% residual activity for recombinant protein, complete loss of activity for native protein
70
-
t1/2: 1.7 min for wild-type enzyme, 30.3 min for mutant enzyme E160G/V198I, 61.4 min for mutant enzyme E160G/V198I/G36S/T103S/A232S/F277Y
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of 0.03 mM FMN increases the stability about 30% after 10 d of storage
-
addition of MnCl2, Dextran 500000, glycerol or octyl glucopyranoside increase stability after 10 d of incubation at 4°C, HgCl2 and SDS destabilizes
-
long chain oxidase stable at -20°C, short chain oxidase stable at -20°C for several months
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isopropanol
-
lactate oxidase retains with more than 60% of it is initial activity after exposing to water-isopropanol mixtures with over 90% v/v content of organic solvent
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, ammonium sulfate precipitate or in solution with 2.5 M glycerol, several months
-
-20°C, lyophilized powder containing 70-80% sucrose, stable for more than a year
-
4°C, 10 mM Tris-HCl, 15 mM NaCl, 0.02 mM FMN, 1 mM EDTA, several weeks, cannot be stored frozen at -20°C or -80°C
-
below 0°C, 0.1 mol/l phosphate buffer, pH 7.2 (potassium and sodium salts), 2.2 mg lactate oxidase in 0.5 ml buffer, enzymatic activity stable for several weeks
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
centrifugation, washing with 10 mM potassium phosphate buffer, pH 6.5, stored at -20°C, resuspended with same buffer, treated with lysozyme followed by disruption with glass beads in a bead mill, centrifugation, supernatants used for enzyme assays
native enzyme from leaves 207fold by ammonium sulfate fractionation, gel filtration, anion exchange chromatography, and again gel filtration
-
native enzyme from maize leaf bundle sheath 46.6fold by gel filtration, anion exchange chromatography, and again gel filtration. Native enzyme 10.5fold from leaf mesophyll, by ammonium sulfate fractionation, gel filtration, anion exchange chromatography, and again gel filtration
-
purified in one step on hydroxyapatite column onto which it is strongly adsorbed. For the initial purification steps, FMN is added to the buffers
-
recombinant enzyme by nickel affinity chromatography, ammonium sulfate fractionation and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BLR DE3 pLysS by nickel affinity chromatography and desalting gel filtration to homogeneity
recombinant His-tagged enzyme from Escherichia coli strain BLR(DE3) pLysS by nickel affinity chromatography and desalting gel filtration to homogeneity
recombinant His-tagged enzyme from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography to high purity
tissue-specific isozymes from leaves 63.5fold by ammonium sulfate fractionation, gel filtration, and anion exchange chromatography, bundle sheath cell isozyme and mesophyll cell isozyme to homogeneity
-
to crystalline state, chromatography and precipitation techniques
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expression of the enzyme with the Rice dwarf virus, RDV, outer capsid P8 protein in Spodoptera frugiperda cells, the localization of P8 in Spodoptera frugiperda cells changed from diffuse to discrete, punctuate inclusions during expression from 24 to 48 h post inoculation, coexpression of GOX with P8 may target P8 into peroxisomes, which serve as replication sites for a number of viruses
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determination of at least five putative GLO gene members in the rice genome, which are located on chromosome 3, 4, and 7, respectively
DNA and amino acid sequence determination and analysis, quantitative expression analysis, the gene contains a GOX-like-riboflavin-5'-phosphate conserved domain and a predicted adenosine-5'-(a-thio)diphospho-5'-ribofuranosylnicotinamide NAD binding domain
expressed in Escherichia coli as a His-tagged fusion protein
expression in Escherichia coli
expression in Escherichia coli. The OcAOD productivity of the recombinant E. coli is 24fold higher than that of Ochrobactrum sp. AIU 033, and it is further enhanced by 1.2 times by the coexpression of additional tatABC from E. coli BL21
-
gene glcD, DNA sequence determination, analysis, and comparison, phylogenetic analysis
gene GO1, DNA and amin acid sequence determination and analysis, phylogenetic tree
-
gene Hao2, isozymes beta1 and beta2, cloning from kidney, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3) using vector pET28a
gene HAO2, quantitative RT-PCR enzyme expression analysis
genes Glo1, sequence comparisons, phylogenetic analysis and tree
genes Glo3, sequence comparisons, phylogenetic analysis and tree, recombinant expression of His-tagged enzyme in Escherichia coli strain BLR (DE3) pLysS
genes Glo4, sequence comparisons, phylogenetic analysis and tree, recombinant expression of His-tagged enzyme in Escherichia coli strain BLR DE3 pLysS
PCR-amplification, expression in Escherichia coli BL21 Star
gene glcD, DNA sequence determination, analysis, and comparison, phylogenetic analysis
-
gene glcD, DNA sequence determination, analysis, and comparison, phylogenetic analysis
-
gene glcD, DNA sequence determination, analysis, and comparison, phylogenetic analysis
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Arabidopsis thaliana plants overexpressing glycolate oxidase in chloroplasts accumulates both hydrogen peroxide and glyoxylate, enzyme-overexpressing plants show retarded development, yellowish rosettes, and impaired photosynthetic performance. The plants develop oxidative stress lesions under photorespiratory conditions but grow like wild-type plants under nonphotorespiratory conditions
expression increases about 65-75% in the booting and heading stages but not in other developmental periods. GLO1 transcripts increase by 60% under PEG treatment
expression is induced by 35% by NaCl treatment
expression is induced by NaCl, abscisic acid, H2O2 and AlCl3 treatments
expression is suppressed by 25-40% under abscisic acid, H2O2 and AlCl3 treatments
expression levels of isoform GLO3 are very low in rice leaves throughout all developmental periods
GLO1 transcripts decrease about 35-40% under NaCl and abscisic acid treatments
the metabolic gene HAO2 is downregulated in hepatocellular carcinoma. Hao2 downregulation is species- and etiology-independent in humans and rodents
the suppression effect of estradiol is dependent on the concentration of estradiol. A reduction of about 60% is observed when 0.001 mM estradiol is applied for 10 d, and the maximal reduction of over 90% occurs at 0.005 mM
the metabolic gene HAO2 is downregulated in hepatocellular carcinoma. Hao2 downregulation is species- and etiology-independent in humans and rodents
the metabolic gene HAO2 is downregulated in hepatocellular carcinoma. Hao2 downregulation is species- and etiology-independent in humans and rodents
the metabolic gene HAO2 is downregulated in hepatocellular carcinoma. Hao2 downregulation is species- and etiology-independent in humans and rodents
the metabolic gene HAO2 is downregulated in hepatocellular carcinoma. Hao2 downregulation is species- and etiology-independent in humans and rodents
-
-
the metabolic gene HAO2 is downregulated in hepatocellular carcinoma. Hao2 downregulation is species- and etiology-independent in humans and rodents
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
inoculation of plants with Pseudomonas syringae increases photorespiration rate and expression of glycolate oxidase (GOX2), serine glyoxylate aminotransferase (SGT) and serine hydroxyl methyltransferase (SHMT1). Silencing of GOX2, SGT or SHMT1 genes in tomato decreases photorespiration but increases susceptibility to Pseudomonas syringae, whereas transient overexpression of GOX2, SGT or SHMT1 in tobacco increases basal defence. Salicylic acid signalling is involved in GOX2-mediated, SGT-mediated and SHMT1-mediated defence. H2O2 pretreatment remarkably alleviates the GOX2 silencing-induced depression in basal defence and salicylic acid signalling
analysis
diagnostics
drug development
medicine
molecular biology
-
the interaction of capsid protein P8 with the GOX of host cells leads to translocation of capsid protein P8 into peroxisomes. The interaction between capsid protein P8 and GOX plays important roles in Rice dwarf phytoreovirus targeting into the replication site of host cells
synthesis
analysis
-
development of a lactate biosensor through immobilization of lactate oxidase in an albumin and mucin composed hydrogel by gluitaraldehyde cross-linking and trapping between two polycarbonate membranes. Hydrogen peroxide produced is detected on a platinum electrode. The response time of the sensor to 0.010 mM lactate requires 90 s to give a 100% steady-state response of 0.079 microA. Linear behavior is obtained between0.7 microM and 1.5 mM. The detection limit calculated from the signal to noise ratio was 0.7 microM
analysis
construction of a D-Lactate electrochemical biosensor. The electrode for detection of D-lactate is prepared by immobilizing dye-linked D-LDH and multi-walled carbon nanotube within Nafion membrane. The electrode response to D-lactate is linear within the concentration range of 0.03-2.5 mM, and it shows little reduction in responsiveness after 50 days
diagnostics
-
lactate biosensor development based on an enzymatic recognition system using lactate oxidase and a transduction system based on laminol, peroxidase from Arthromyces ramosus and metallic aluminum, immobilized in a plastic support by a polyion complex membrane prepared from poly-L-lysine hydrobromide and poly(sodium 4-styrenesulfonate)
diagnostics
-
lactate biosensor (FIA amperometric detection), tested with beer samples, detection limit: 0.84 micromol/l, three-electrode cell with AG/AGCl, NaCl reference electrode, platinum wire, glassy carbon electrode, the latter layered with Prussian Blue film of K3Fe(CN)6, Fe(III), KCl, cetyltrimethylammonium bromide, pH 1.7 maintained with HCl, lactate oxidase immobilized onto the Prussian Blue-modified glassy carbon electrode, enzyme layer covered by a Nafion-ethanol solution, storage in phosphate buffer, pH 6.9
diagnostics
the metabolic gene HAO2 is downregulated in hepatocellular carcinoma and predicts metastasis and poor survival. Dysregulation of HAO2 is a very early event in the development of hepatocellular carcinoma and it may represent a useful diagnostic and prognostic marker for human hepatocellular carcinoma
drug development
in humans the enzyme is a potential drug target for treatment of primary hyperoxaluria, a genetic disorder where overproduction of oxalate results in the formation of kidney stones
drug development
-
isozyme Hao2 is a target for drug development in high blood pressure
medicine
-
enzyme is used in clinical chemistry for the determination of (S)-lactate in blood in some pathological diseases such as diabetes, heart diseases and shock syndrome
medicine
-
decrease of enzyme activity upon oxidative stress induced by glutathione depletion or postischemic perfusion, down-regulation of enzyme as mechanism to prevent excessive H2O2 formation in liver peroxisome
medicine
the ability of such siRNAs to reduce urinary oxalate in the mouse model suggests that this approach is promising for the treatment of primary hyperoxalurias, PH, particularly PH type I, in humans, genes HYPDH and GO appear to be the best targets for reducing the production of glyoxylate and oxalate in PH patients
medicine
application of oan in vivo CRISPR/Cas9-mediated substrate reduction therapy to treat primary hyperoxaluria type I that results in excessive hepatic oxalate production causing end-stage renal disease. A single systemic administration of an AAV8-CRISPR/Cas9 vector targeting glycolate oxidase, prevents oxalate overproduction and kidney damage, with no signs of toxicity in Agxt1-/- mice
medicine
-
the ability of such siRNAs to reduce urinary oxalate in the mouse model suggests that this approach is promising for the treatment of primary hyperoxalurias, PH, particularly PH type I, in humans, genes HYPDH and GO appear to be the best targets for reducing the production of glyoxylate and oxalate in PH patients
-
synthesis
-
production of glyoxylate in biocatalysis of co-produced glycolate oxidase and catalase T
synthesis
-
optimization of enzyme expression in Escherichia coli for production glyoxylate in culture medium
synthesis
-
optimization of production of lactate oxidase by cultivating strains under high aeration in a medium with 0.5% glucose and 2% lactate for 1 day results in activities of 130-140 U/l
synthesis
coexpression of N-demethylase NdmB gene from Pseudomonas putida CBB5 and glycolate oxidase gene in Escherichia coli. By two-step purification of Ni affinity chromatography and Q-Sepharose chromatography, the coexpressed NdmB and GO are separated and result in a 15.8fold purification with 8.7% yield and 12.8fold purification with 7.2% yield, respectively
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Arabidopsis thaliana (Q9LJH5), Arabidopsis thaliana (Q24JJ8), Arabidopsis thaliana (Q9LRR9)
brenda
Dutta, C.; Avitahl-Curtis, N.; Pursell, N.; Larsson Cohen, M.; Holmes, B.; Diwanji, R.; Zhou, W.; Apponi, L.; Koser, M.; Ying, B.; Chen, D.; Shui, X.; Saxena, U.; Cyr, W.A.; Shah, A.; Nazef, N.; Wang, W.; Abrams, M.; Dudek, H.; Salido, E.; Brown, B.D.; Lai, C.
Inhibition of glycolate oxidase with dicer-substrate siRNA reduces calcium oxalate deposition in a mouse model of primary hyperoxaluria type 1
Mol. Ther.
24
770-778
2016
Mus musculus (Q9WU19), Mus musculus, Mus musculus C57BL/6 (Q9WU19)
brenda
Satomura, T.; Hayashi, J.; Sakamoto, H.; Nunoura, T.; Takaki, Y.; Takai, K.; Takami, H.; Ohshima, T.; Sakuraba, H.; Suye, S.I.
D-Lactate electrochemical biosensor prepared by immobilization of thermostabledye-linked D-lactate dehydrogenase from Candidatus Caldiarchaeum subterraneum
J. Biosci. Bioeng.
126
425-430
2018
Candidatus Caldarchaeum subterraneum (E6N788)
brenda
Liu, Y.; Wu, W.; Chen, Z.
Structures of glycolate oxidase from Nicotiana benthamiana reveal a conserved pH sensor affecting the binding of FMN
Biochem. Biophys. Res. Commun.
503
3050-3056
2018
Nicotiana benthamiana (E1AXT8), Nicotiana benthamiana
brenda
Zhang, Z.; Li, X.; Cui, L.; Meng, S.; Ye, N.; Peng, X.
Catalytic and functional aspects of different isozymes of glycolate oxidase in rice
BMC Plant Biol.
17
135
2017
Oryza sativa Japonica Group (Q10CE4), Oryza sativa Japonica Group (Q7FAS1), Oryza sativa Japonica Group (Q8H3I4)
brenda
Matsumura, K.; Yamada, M.; Yamashita, T.; Muto, H.; Nishiyama, K.I.; Shimoi, H.; Isobe, K.
Expression of alcohol oxidase gene from Ochrobactrum sp. AIU 033 in recombinant Escherichia coli through the twin-arginine translocation pathway
J. Biosci. Bioeng.
128
13-21
2019
Ochrobactrum sp. AIU 033
brenda
Li, D.; Han, Q.; Zhang, T.
Cloning and coexpression of recombinant N-demethylase B and glycolate oxidase genes in Escherichia coli
Mol. Biol. Rep.
46
505-510
2019
Spinacia oleracea (P05414), Spinacia oleracea
brenda
Yang, M.; Li, Z.; Zhang, K.; Zhang, X.; Zhang, Y.; Wang, X.; Han, C.; Yu, J.; Xu, K.; Li, D.
Barley stripe mosaic virus gammab interacts with glycolate oxidase and inhibits peroxisomal ROS production to facilitate virus infection
Mol. Plant
11
338-341
2018
Nicotiana benthamiana (E1AXT8)
brenda
Zabaleta, N.; Barberia, M.; Martin-Higueras, C.; Zapata-Linares, N.; Betancor, I.; Rodriguez, S.; Martinez-Turrillas, R.; Torella, L.; Vales, A.; Olaguee, C.; Vilas-Zornoza, A.; Castro-Labrador, L.; Lara-Astiaso, D.; Prosper, F.; Salido, E.; Gonzalez-Aseguinolaza, G.; Rodriguez-Madoz, J.R.
CRISPR/Cas9-mediated glycolate oxidase disruption is an efficacious and safe treatment for primary hyperoxaluria type I
Nat. Commun.
9
5454
2018
Mus musculus (Q9WU19)
brenda
Ahammed, G.J.; Li, X.; Zhang, G.; Zhang, H.; Shi, J.; Pan, C.; Yu, J.; Shi, K.
Tomato photorespiratory glycolate-oxidase-derived H2O2 production contributes to basal defence against Pseudomonas syringae
Plant Cell Environ.
41
1126-1138
2018
Solanum lycopersicum
brenda
Schmitz, J.; Huedig, M.; Meier, D.; Linka, N.; Maurino, V.G.
The genome of Ricinus communis encodes a single glycolate oxidase with different functions in photosynthetic and heterotrophic organs
Planta
252
100
2020
Ricinus communis (B9ST74), Ricinus communis (B9S0Y9), Ricinus communis
brenda
Xu, Y.P.; Yang, J.; Cai, X.Z.
Glycolate oxidase gene family in Nicotiana benthamiana genome-wide identification and functional analyses in disease resistance
Sci. Rep.
8
8615
2018
Nicotiana benthamiana
brenda
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