Any feedback?
No. of entries
Information on EC 1.3.2.3 - L-galactonolactone dehydrogenase
for references in articles please use BRENDA:EC1.3.2.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.3 Acting on the CH-CH group of donors
1.3.2 With a cytochrome as acceptor
1.3.2.3 L-galactonolactone dehydrogenase
IUBMB Comments
This enzyme catalyses the final step in the biosynthesis of L-ascorbic acid in higher plants and in nearly all higher animals with the exception of primates and some birds . The enzyme is very specific for its substrate L-galactono-1,4-lactone as D-galactono-γ-lactone, D-gulono-γ-lactone, L-gulono-γ-lactone, D-erythronic-γ-lactone, D-xylonic-γ-lactone, L-mannono-γ-lactone, D-galactonate, D-glucuronate and D-gluconate are not substrates . FAD, NAD+, NADP+ and O2 (cf. EC 1.3.3.12, L-galactonolactone oxidase) cannot act as electron acceptor .
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.3.2.3
- asa
- l-galactose
- dehydroascorbate
- monodehydroascorbate
-
l-galactose-1-phosphate
- l-gulono-1,4-lactone
- galdh
- gdp-d-mannose
- mdhar
- gdp-l-galactose
- aldonolactone
- d-galacturonate
-
ascorbate-glutathione
-
smirnoff-wheeler
Reaction Schemes
showSynonyms
l-galactono-1,4-lactone dehydrogenase, galldh, l-galactono-gamma-lactone dehydrogenase, ferricytochrome c oxidoreductase, l-galldh, gldhase, galactono-1,4-lactone dehydrogenase, gldase, l-galactonolactone dehydrogenase, galactonolactone dehydrogenase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, galactonolactone
-
-
-
-
GALDH
GalLDH
GLDH
GLDHase
L-galactono-1,4-lactone dehydrogenase
L-galactono-gamma-lactone dehydrogenase
L-GalLDH
L-galactono-1,4-lactone dehydrogenase
-
-
L-galactono-gamma-lactone dehydrogenase
-
-
-
-
L-galactono-gamma-lactone dehydrogenase
-
catalyzes the final step in the biosynthesis of vitamin C in plants
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-galactono-1,4-lactone + 2 ferricytochrome c = L-ascorbate + 2 ferrocytochrome c + 2 H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
L-ascorbate biosynthesis I (plants, L-galactose pathway), L-ascorbate biosynthesis VII (plants, D-galacturonate pathway)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
L-galactono-1,4-lactone:ferricytochrome-c oxidoreductase
This enzyme catalyses the final step in the biosynthesis of L-ascorbic acid in higher plants and in nearly all higher animals with the exception of primates and some birds [5]. The enzyme is very specific for its substrate L-galactono-1,4-lactone as D-galactono-gamma-lactone, D-gulono-gamma-lactone, L-gulono-gamma-lactone, D-erythronic-gamma-lactone, D-xylonic-gamma-lactone, L-mannono-gamma-lactone, D-galactonate, D-glucuronate and D-gluconate are not substrates [5]. FAD, NAD+, NADP+ and O2 (cf. EC 1.3.3.12, L-galactonolactone oxidase) cannot act as electron acceptor [5].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9029-02-1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-arabinono-1,4-lactone + ferrocytochrome c + H+
?
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + 1,4-benzoquinone
L-ascorbate + reduced 1,4-benzoquinone
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
L-galactono-1,4-lactone + phenazine methosulfate
L-ascorbate + reduced phenazine methosulfate
-
Substrates: -
Products: -
Products: -
?
L-gulono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
L-mannono-gamma-lactone + ferricytochrome c
D-ascorbate + ferricytochrome c
-
Substrates: 18% activity of that with L-galactono-gamma-lactone
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
Substrates: final enzyme in synthesis of ascorbic acid
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
Substrates: terminal step in L-ascorbic acid biosynthesis
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
Substrates: terminal step in L-ascorbic acid biosynthesis
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
Substrates: terminal step in L-ascorbic acid biosynthesis
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
Substrates: ascorbic acid biosynthesis precursors are L-galactono-gamma-lactone and L-gulono-gamma-lactone
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
Substrates: activity is inducible by addition of D-glucose, D-galactose or L-gulono-gamma-lactone in vivo
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
Substrates: terminal step in L-ascorbic acid biosynthesis
Products: -
Products: -
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
Substrates: overall reaction
Products: -
Products: -
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
Substrates: overall reaction
Products: -
Products: -
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
Substrates: overall reaction
Products: -
Products: -
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
Substrates: overall reaction
Products: -
Products: -
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
Substrates: overall reaction
Products: -
Products: -
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
Substrates: overall reaction
Products: -
Products: -
?
L-galactono-1,4-lactone + cytochrome c
L-ascorbate + reduced cytochrome c
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + cytochrome c
L-ascorbate + reduced cytochrome c
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + cytochrome c
L-ascorbate + reduced cytochrome c
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
Substrates: specific for cytochrome c as electron acceptor
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
Substrates: native and recombinant from yeast
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: reduces only phenazine methosulfate and cytochrome c
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: specific for L-galactono-gamma-lactone
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
Substrates: specific for L-galactono-gamma-lactone
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
Substrates: final enzyme in synthesis of ascorbic acid, expression is regulated by light
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
Substrates: infiltration of the substrate through the fruit petiole at the small green and turning stage results in a 50% increase in total L-ascorbate content, but in no differences in enzyme activity and expression
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: specific for L-galactono-gamma-lactone
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: final enzyme in synthesis of ascorbic acid
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: native and recombinant enzyme
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: specific for L-galactono-gamma-lactone
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: specific for cytochrome c as electron acceptor
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: final enzyme in synthesis of ascorbic acid
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: final enzyme in synthesis of ascorbic acid. L-Galactono-gamma-lactone dehydrogenase and vitamin C content in fresh-cut potatoes stored under controlled atmospheres: fresh-cutting provoces an increase in enzyme activity in potato strips in all atmospheres tested. Highest induction, 15.5fold, is observed in strips stored in air
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: the pI 4.3 enzyme form is much more effective than that of potato tuber pI 5 enzyme to catalyze the synthesis of ascorbic acid
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: reduces only phenazine methosulfate and cytochrome c
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: specific for L-galactono-gamma-lactone
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c + H+
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c + H+
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c + H+
-
Substrates: -
Products: -
Products: -
r
L-gulono-gamma-lactone + ferricytochrome
D-ascorbate + ferricytochrome c
-
Substrates: very low activity
Products: -
Products: -
?
L-gulono-gamma-lactone + ferricytochrome
D-ascorbate + ferricytochrome c
-
Substrates: recombinant enzyme: 7% activity of the activity with L-galactono-gamma-lactone
Products: -
Products: -
?
L-gulono-gamma-lactone + ferricytochrome
D-ascorbate + ferricytochrome c
-
Substrates: 23% activity of that with L-galactono-gamma-lactone
Products: -
Products: -
?
additional information
?
-
-
Substrates: D-galactono-1,4-lactone, D-gulono-1,4-lactone, L-mannono-1,4-lactone, and D-galacturonic acid are no substrates, molecular oxygen can not serve as efficient electron acceptor for the mutant enzymes
Products: -
Products: -
?
additional information
?
-
-
Substrates: a kinetic and thermodynamic study of the GALDH-cytochrome c interaction and electron-transfer reactions by using laser-flash photolysis and stopped-flow kinetic analysis as well as isothermal titration calorimetry (ITC) and NMR spectroscopy are performed. Results show a transient, highly dynamic GALDH- cytochrome c interaction, similar for all partner redox states
Products: -
Products: -
?
additional information
?
-
-
Substrates: incubation of leaf discs in a L-galactonolactone solution leads to a rapid 2 to 3fold increase in the L-ascorbate content in both GLDH-transformed and non-transformed plants in the same manner
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
L-galactono-1,4-lactone + cytochrome c
L-ascorbate + reduced cytochrome c
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: incubation of leaf discs in a L-galactonolactone solution leads to a rapid 2 to 3fold increase in the L-ascorbate content in both GLDH-transformed and non-transformed plants in the same manner
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
Substrates: final enzyme in synthesis of ascorbic acid
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
Substrates: terminal step in L-ascorbic acid biosynthesis
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
Substrates: terminal step in L-ascorbic acid biosynthesis
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
Substrates: terminal step in L-ascorbic acid biosynthesis
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
Substrates: ascorbic acid biosynthesis precursors are L-galactono-gamma-lactone and L-gulono-gamma-lactone
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
Substrates: activity is inducible by addition of D-glucose, D-galactose or L-gulono-gamma-lactone in vivo
Products: -
Products: -
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
Substrates: terminal step in L-ascorbic acid biosynthesis
Products: -
Products: -
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
Substrates: overall reaction
Products: -
Products: -
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
Substrates: overall reaction
Products: -
Products: -
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
Substrates: overall reaction
Products: -
Products: -
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
Substrates: overall reaction
Products: -
Products: -
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
Substrates: overall reaction
Products: -
Products: -
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
Substrates: overall reaction
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
Substrates: final enzyme in synthesis of ascorbic acid, expression is regulated by light
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: final enzyme in synthesis of ascorbic acid
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: final enzyme in synthesis of ascorbic acid
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
Substrates: final enzyme in synthesis of ascorbic acid. L-Galactono-gamma-lactone dehydrogenase and vitamin C content in fresh-cut potatoes stored under controlled atmospheres: fresh-cutting provoces an increase in enzyme activity in potato strips in all atmospheres tested. Highest induction, 15.5fold, is observed in strips stored in air
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c + H+
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c + H+
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
a putative N-terminal FAD-binding domain localizes between residues 128 and 264, wherein is located a motif 157VGSGLSP163 common to L-GalLDHs characterized from plants
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Mg2+, Ca2+ and Sr2+ have no effect on activity
additional information
-
Mg2+, Ca2+ and Sr2+ have no effect on activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Atebrin
-
reaction with ferricytochrome inhibited, reaction with phenazine methosulfate not
glutathione
the enzyme activity is inhibited by 60% by reduced glutathione (GSH)
H2O2
GALDH is inactivated by hydrogen peroxide due to selective oxidation of cysteine 340, located in the cap domain
phosphate
-
reaction with ferricytochrome inhibited, reaction with phenazine methosulfate stimulated
riboflavin
-
reaction with ferricytochrome inhibited, reaction with phenazine methosulfate not
L-galactono-gamma-lactone
substrate inhibition at concentration above 32.6 mM
L-galactono-gamma-lactone
-
substrate inhibition at concentration above 4.2 mM
additional information
-
no substrate inhibition with L-gulono-1,4-lactone at concentrations up to 100 mM, D-galactono-1,4-lactone, D-gulono-1,4-lactone, L-mannono-1,4-lactone, and D-galacturonic acid do not inhibit the oxidation of L-galactono-1,4-lactone, no specific inhibition by cations or anions is observed
-
additional information
-
the transcript levels of L-galactono-1,4-lactone dehydrogenase is down-regulated in the dark
-
additional information
no inhibition with riboflavin and lycorine
-
additional information
-
no inhibition with riboflavin and lycorine
-
additional information
incubation of pepper crude extracts with increasing concentrations of SIN-1, a peroxynitrite donor, does not modify GalLDH activity significantly. Similarly, S-nitrosoglutathione, GSNO, an NO donor, does not affect the enzyme activity either
-
additional information
the RNAi-reduced expression of GalLDH leads to up to 80% reduction in activity
-
additional information
-
the RNAi-reduced expression of GalLDH leads to up to 80% reduction in activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
drought
-
causes a substantial increase in GalLDH protein and activity in the low ascorbic acid cultivar Cooperativa Maipún, but has no effect in higher ascorbic acid cultivar Buck Chambergo
-
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
Ascorbic Acid Deficiency
Ascorbic acid deficiency leads to increased grain chalkiness in transgenic rice for suppressed of L-GalLDH.
Dehydration
Jasmonic acid regulates ascorbate and glutathione metabolism in Agropyron cristatum leaves under water stress
Infections
The effect of Botrytis cinerea infection on the antioxidant profile of mitochondria from tomato leaves.
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
0.28
1,4-benzoquinone
-
wild type enzyme, in the presence of L-galactono-1,4-lactone, in 50 mM sodium phosphate (pH 8.8), at 25°C
0.034
cytochrome c
-
wild type enzyme, in the presence of L-galactono-1,4-lactone, in 50 mM sodium phosphate (pH 8.8), at 25°C
0.026
phenazine methosulfate
-
wild type enzyme, in the presence of L-galactono-1,4-lactone, in 50 mM sodium phosphate (pH 8.8), at 25°C
0.061
L-galactono-1,4-lactone
recombinant wild-type TaGLDH-A1a variant, pH 8.0, temperature not specified in the publication
0.12
L-galactono-1,4-lactone
-
mutant enzyme L56H, in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C
0.17
L-galactono-1,4-lactone
-
wild type enzyme, in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C
0.181
L-galactono-1,4-lactone
recombinant mutant TaGLDH-A1b variant, pH 8.0, temperature not specified in the publication
0.32
L-galactono-1,4-lactone
-
mutant enzyme L56I, in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C
0.56
L-galactono-1,4-lactone
-
mutant enzyme L56F in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C
0.99
L-galactono-1,4-lactone
-
mutant enzyme L56C, in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C
1.7
L-galactono-1,4-lactone
-
mutant enzyme L56IA in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C