Any feedback?
No. of entries
Information on EC 1.1.1.45 - L-gulonate 3-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.45
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.45 L-gulonate 3-dehydrogenase
IUBMB Comments
Also oxidizes other L-3-hydroxyacids.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 1.1.1.45
-
protomer
-
uronate
- medicine
- drosophila
- lens
- acetoacetate
-
dehydrogenation
showSynonyms
l-beta-hydroxyacid dehydrogenase, l-gulonate 3-dehydrogenase, l-3-hydroxyacid dehydrogenase, l-gulonic acid 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
L-3-aldonate dehydrogenase
-
-
-
-
L-3-aldonic dehydrogenase
-
-
-
-
L-3-hydroxyacid dehydrogenase
-
-
-
-
L-beta-hydroxy-acid-NAD-oxidoreductase
-
-
-
-
L-beta-hydroxyacid dehydrogenase
-
-
-
-
L-gulonic acid dehydrogenase
-
-
-
-
additional information
the enzyme belongs to the GDH/lambdaCRY family
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-gulonate + NAD+ = 3-dehydro-L-gulonate + NADH + H+
-
-
-
-
L-gulonate + NAD+ = 3-dehydro-L-gulonate + NADH + H+
Cys125, Glu97, and Ser124 are putative coenzyme/substrate-binding residues, catalytic mechanism with induced-fit mechanism upon coenzyme binding and involving a network-based substrate recognition, overview
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
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
MetaCyc
D-glucuronate degradation I
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
L-gulonate:NAD+ 3-oxidoreductase
Also oxidizes other L-3-hydroxyacids.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9028-51-7
-
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
2-keto-L-gulonate + NADH
2,3-diketo-L-gulonate + NAD+
-
Substrates: -
Products: -
Products: -
ir
DL-3-hydroxybutanoate + NADH + H+
acetoacetate + NAD+
-
Substrates: -
Products: -
Products: -
r
L-gulonate + NADP+
3-dehydro-L-gulonate + NADPH + H+
Substrates: NAD+ is preferred as cofactor
Products: -
Products: -
r
L-3-hydroxybutanoate + NADH
acetoacetate + NAD+
-
Substrates: -
Products: -
Products: -
r
L-3-hydroxybutanoate + NADH
acetoacetate + NAD+
-
Substrates: -
Products: -
Products: -
?
L-gulonate + NAD+
3-dehydro-L-gulonate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-gulonate + NAD+
3-dehydro-L-gulonate + NADH + H+
Substrates: -
Products: -
Products: -
r
L-gulonate + NAD+
3-dehydro-L-gulonate + NADH + H+
Substrates: NAD+ is preferred as cofactor
Products: -
Products: -
r
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
Substrates: glucuronate-xylulose cycle
Products: -
Products: -
?
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
Substrates: glucuronate-xylulose cycle
Products: -
Products: -
?
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
Substrates: stereospecificity for L-configuration of the beta-carbon hydroxyl group
Products: -
Products: -
r
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
Substrates: glucuronate-xylulose cycle
Products: -
Products: -
?
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
Substrates: stereospecificity for L-configuration of the beta-carbon hydroxyl group
Products: -
Products: -
r
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
Substrates: glucuronate-xylulose cycle
Products: -
Products: -
r
additional information
?
-
-
Substrates: no substrates are: DL-2-hydroxybutanoate, DL-4-hydroxybutanoate, 2-butanol, DL-3-hydroxypropionate, L-threonine
Products: -
Products: -
?
additional information
?
-
Substrates: active site structure and substrate recognition, importance of the dimeric state of the enzyme, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: active site structure and substrate recognition, importance of the dimeric state of the enzyme, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates are: L-arabonic acid, D-glucuronate, D-mannuronate, l-iduronate, 6-phospho-D-gluconate, L-serine, L-threonine, beta-D-hydroxy acids, acetoacetyl-CoA, acetoacetyl-S-pantetheine
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-gulonate + NAD+
3-dehydro-L-gulonate + NADH + H+
Substrates: -
Products: -
Products: -
r
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
Substrates: glucuronate-xylulose cycle
Products: -
Products: -
?
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
Substrates: glucuronate-xylulose cycle
Products: -
Products: -
?
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
Substrates: glucuronate-xylulose cycle
Products: -
Products: -
?
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
Substrates: glucuronate-xylulose cycle
Products: -
Products: -
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
no activation or inhibition Zn2+, Cd2+, Cu2+, Fe3+, Mn2+, Ni2+, Co3+, As3+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbic acid
-
molecular dockings of ascorbate to gulonate-3-dehydrogenase indicated its binding near the co-factor binding site. Docking revealed that ascorbate binding could lead to steric clashes between ascorbate and the co-factor (NADH)
additional information
-
no inhibition by 20 mM D-glucose, 2 mM 2-keto-L-gulonate, 1 mM D-glucorunate or 6 mM ADP, ATP and AMP; no significant inhibition (less than 15%) by 1 mM L-ascorbate, monocarboxylic acids, or dicarboxylic acids
-
additional information
-
not inhibitory iodoacetate, ethylendiamine tetraacetate, 2,2'-bipyridine, 8-hydroxyquiniline, O-phenanthroline, diethyldithiocarbamate, thiamine pyrophosphate
-
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
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
2.6
L-gulonate
with NADP+, mutant enzyme D36R/Q41N, pH 7.0, 25°C
additional information
additional information
-
no activity with 5-40 mM sugars or hydroxyacids like 2-keto-L-guluonate, 3-deoxyglucosone, xylitol, L-threitol, ascorbic acid, malic acid, L-threonine, L-glycerate, L-tartarate and L-lactate, or 50 mM ethyl and methyl esters of 3-hydroxybutyrate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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
metabolism
-
crucial enzyme in the non-phosphorylated sugar metabolism or glucuronate-xylulose pathway
physiological function
L-gulonate 3-dehydrogenase is a bifunctional dimeric protein that functions not only as an NAD+-dependent enzyme in the uronate cycle but also as a taxon-specific lambda-crystallin in rabbit lens
Show AA Sequence and Transmembrane Helices (2632 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
60000 - 70000
36000
-
X-ray diffraction, natural active protein is presumably a dimer 2 * 36000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
-
X-ray diffraction, natural active protein is presumably a dimer 2 * 36000
additional information
additional information
the enzyme possesses two domains, the N-terminal domain with a Rossmann fold and the C-terminal domain with a helical fold. In the N-terminal domain of the NADH-bound structure exist 11 coenzyme-binding residues and two distinct side-chain conformers of coenzyme binding residue Ser124. Subunit dimerization is mediated by numerous intersubunit interactions, including 22 hydrogen bonds and 104 residue pairs of van der Waals interactions, of which those between two cognate C-terminal domains are predominant. Domain and subunit interface structures, structure comparison with the human enzyme, overview
additional information
-
the enzyme possesses two domains, the N-terminal domain with a Rossmann fold and the C-terminal domain with a helical fold. In the N-terminal domain of the NADH-bound structure exist 11 coenzyme-binding residues and two distinct side-chain conformers of coenzyme binding residue Ser124. Subunit dimerization is mediated by numerous intersubunit interactions, including 22 hydrogen bonds and 104 residue pairs of van der Waals interactions, of which those between two cognate C-terminal domains are predominant. Domain and subunit interface structures, structure comparison with the human enzyme, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme in both apo form and NADH-bound holo form, X-ray diffraction structure determination and analysis at 1.70-1.85 A resolution
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D36R
D36R/Q41N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E97Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q41N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D36R
-
mutation leads to a switch in the favor of NADP(H) specificity, suggesting an important role of Asp36 in the coenzyme specificity
D36R
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
in solution instable, by addition of below mM of cyanide several days in the cold, minor effect through EDTA-addition
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation, Sephadex G-100 column chromatography, Q-Sepharose column chromatography, Blue-Sepharose column chromatography, hydroxylapatite column chromatography
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) cells
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) cells
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
role in an alternative pathway of the production of xylitol in the lens that causes cataracts in mammalian organisms
medicine
-
role in an alternative pathway of the production of xylitol in the lens that causes cataracts in mammalian organisms
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Goode, D.; Lewis, M.E.; Crabbe, M.J.C.
Accumulation of xylitol in the mammalian lens is realted to glucoronate metabolism
FEBS Lett.
395
174-178
1996
Bos taurus, Rattus norvegicus
brenda
Smiley, J.D.; Ashwell, G.
Purification and properties of beta-L-hydroxy acid dehydrogenase
J. Biol. Chem.
236
357-364
1961
Sus scrofa
-
brenda
Dworsky, P.; Hoffmann-Ostenhof, O.
L-3-Aldonic acid dehydrogenase from Schwanniomyces occidentalis
Acta Biochim. Pol.
9
269-277
1964
Schwanniomyces occidentalis
-
brenda
Borack, L.I.; Sofer, W.
Drosophila beta-L-hydroxy acid dehydrogenase
J. Biol. Chem.
246
5345-5350
1970
Drosophila melanogaster
brenda
Koundakjian, P.P.; Snoswell, A.M.
3-Hydroxy acid dehydrogenases in Sheep tissues
Biochem. J.
127
449-452
1972
Ovis aries
brenda
Borack, L.I.
Organ distribution of Drosophila L-3-hydroxyacid: NAD oxidase
Experientia
30
31
1974
Drosophila melanogaster
-
brenda
Cannistraro, V.J.; Borack, L.I.; Chase, T.
Subunit structure and kinetic properties of L-beta-hydroxyacid dehydrogenase of Drosophila
Biochim. Biophys. Acta
569
1-5
1979
Drosophila melanogaster
brenda
Menotti-Raymond, M.; Sullivan, D.T.
Further characterization of L-beta-hydroxyacid dehydrogenase from Drosophila
Biochim. Biophys. Acta
841
15-21
1985
Drosophila melanogaster
brenda
Ishikura, S.; Usami, N.; Araki, M.; Hara, A.
Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase
J. Biochem.
137
303-314
2005
Oryctolagus cuniculus
brenda
Asada, Y.; Kuroishi, C.; Ukita, Y.; Sumii, R.; Endo, S.; Matsunaga, T.; Hara, A.; Kunishima, N.
Crystallization and preliminary X-ray crystallographic analysis of rabbit L-gulonate 3-dehydrogenase
Acta Crystallogr. Sect. F
64
228-230
2008
Oryctolagus cuniculus
brenda
Asada, Y.; Kuroishi, C.; Ukita, Y.; Sumii, R.; Endo, S.; Matsunaga, T.; Hara, A.; Kunishima, N.
Dimeric crystal structure of rabbit L-gulonate 3-dehydrogenase/lambda-crystallin: insights into the catalytic mechanism
J. Mol. Biol.
401
906-920
2010
Oryctolagus cuniculus (P14755), Oryctolagus cuniculus
brenda
Agrawal, N.; Hossain, M.S.; Skelton, A.A.; Muralidhar, K.; Kaushik, S.
Unraveling the mechanism of L-gulonate-3-dehydrogenase inhibition by ascorbic acid insights from molecular modeling
Comput. Biol. Chem.
77
146-153
2018
Bubalus bubalis
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.45)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
