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EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
l-gulonate 3-dehydrogenase, l-beta-hydroxyacid dehydrogenase, l-3-hydroxyacid dehydrogenase, l-gulonic acid dehydrogenase,
more
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L-3-aldonate dehydrogenase
-
-
-
-
L-3-aldonic dehydrogenase
-
-
-
-
L-3-hydroxyacid dehydrogenase
-
-
-
-
L-beta-hydroxy-acid-NAD-oxidoreductase
-
-
-
-
L-beta-hydroxyacid dehydrogenase
-
-
-
-
L-gulonate 3-dehydrogenase
-
-
L-gulonic acid dehydrogenase
-
-
-
-
additional information
the enzyme belongs to the GDH/lambdaCRY family
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L-gulonate + NAD+ = 3-dehydro-L-gulonate + NADH + H+
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
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L-gulonate:NAD+ 3-oxidoreductase
Also oxidizes other L-3-hydroxyacids.
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2-keto-L-gulonate + NADH
2,3-diketo-L-gulonate + NAD+
-
-
-
-
ir
? + NADP+
? + NADPH
-
-
-
-
?
acetoacetate + NADH
? + NAD+
-
-
-
-
?
D-galactonic acid + NAD+
?
-
-
-
-
?
D-mannonic acid + NAD+
?
-
-
-
-
?
D-talonic acid + NAD+
?
-
-
-
-
?
D-xylonic acid + NAD+
?
-
-
-
-
?
DL-3-hydroxybutanoate + NADH + H+
acetoacetate + NAD+
-
-
-
-
r
L-3-hydroxybutanoate + NADH
acetoacetate + NAD+
L-3-hydroxybutyrate + ?
?
-
-
-
-
?
L-altronic acid + NAD+
?
-
-
-
-
?
L-erythronic acid + NAD+
?
-
-
-
-
?
L-gulonate + NAD+
3-dehydro-L-gulonate + NADH + H+
L-gulonate + NADP+
3-dehydro-L-gulonate + NADPH + H+
NAD+ is preferred as cofactor
-
-
r
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
L-ribonic acid + NAD+
?
-
-
-
-
?
L-threonate + ?
?
-
-
-
-
?
L-threonic acid + NAD+
?
-
-
-
-
?
additional information
?
-
D-gluconic acid + NAD+
?
-
-
-
-
?
D-gluconic acid + NAD+
?
-
-
-
-
?
D-lyxonic acid + NAD+
?
-
-
-
-
?
D-lyxonic acid + NAD+
?
-
-
-
-
?
L-3-hydroxybutanoate + NADH
acetoacetate + NAD+
-
-
-
-
?
L-3-hydroxybutanoate + NADH
acetoacetate + NAD+
-
-
-
-
r
L-3-hydroxybutanoate + NADH
acetoacetate + NAD+
-
-
-
-
r
L-3-hydroxybutanoate + NADH
acetoacetate + NAD+
-
-
-
-
r
L-gulonate + NAD+
3-dehydro-L-gulonate + NADH + H+
-
-
-
-
?
L-gulonate + NAD+
3-dehydro-L-gulonate + NADH + H+
-
-
-
r
L-gulonate + NAD+
3-dehydro-L-gulonate + NADH + H+
NAD+ is preferred as cofactor
-
-
r
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
-
-
-
r
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
glucuronate-xylulose cycle
-
-
?
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
-
-
-
?
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
-
-
-
r
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
-
-
-
r
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
glucuronate-xylulose cycle
-
-
?
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
stereospecificity for L-configuration of the beta-carbon hydroxyl group
-
-
r
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
glucuronate-xylulose cycle
-
-
?
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
stereospecificity for L-configuration of the beta-carbon hydroxyl group
-
-
r
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
glucuronate-xylulose cycle
-
r
L-idonic acid + NAD+
?
-
-
-
-
?
L-idonic acid + NAD+
?
-
-
-
-
?
additional information
?
-
-
no substrates are: DL-2-hydroxybutanoate, DL-4-hydroxybutanoate, 2-butanol, DL-3-hydroxypropionate, L-threonine
-
-
?
additional information
?
-
active site structure and substrate recognition, importance of the dimeric state of the enzyme, overview
-
-
?
additional information
?
-
-
active site structure and substrate recognition, importance of the dimeric state of the enzyme, overview
-
-
?
additional information
?
-
-
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
-
-
?
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L-gulonate + NAD+
3-dehydro-L-gulonate + NADH + H+
-
-
-
r
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
glucuronate-xylulose cycle
-
-
?
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
-
-
-
?
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
glucuronate-xylulose cycle
-
-
?
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
glucuronate-xylulose cycle
-
-
?
L-gulonic acid + NAD+
3-dehydro-L-gulonic acid + NADH + H+
-
glucuronate-xylulose cycle
-
r
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NADPH
cofactor binding mode, overview
NAD+
-
-
NAD+
cofactor binding mode, overview
NADH
-
-
NADH
cofactor binding mode, overview
NADP+
-
-
NADP+
-
10% activity of NAD+
NADP+
cofactor binding mode, overview
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additional information
-
no activation or inhibition Zn2+, Cd2+, Cu2+, Fe3+, Mn2+, Ni2+, Co3+, As3+
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acetoacetate
-
competitive inhibitor
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)
Cibacron blue
-
competitive inhibition with respect to NAD+
malonate
-
reversible inhibition, IC50: 0.34 mM
malonic acid monoethyl ester
-
weak inhibition, IC50: 5.5 mM
NADH
-
competitive inhibitor
p-chloromercuriphenylsulfonate
-
0.001 mM, complete inhibition
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
in both directions
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
-
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cysteine
-
in mM-concentration, no activation of the reverse reaction
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7.3
2,3-diketo-L-gulonate
-
cofactor NADH, pH 6.3
0.45
beta-keto-L-gulonate
-
cofactor NADH, pH 6.3
19
D-gluconate
-
cofactor NAD+, pH 8.5
5.3 - 22.8
L-3-hydroxybutanoate
2.2 - 2.3
L-3-hydroxybutyrate
5.3
L-Idonate
-
cofactor NAD+, pH 8.5
additional information
additional information
-
6.4
acetoacetate
-
cofactor NADH, pH 6.3
8.3
acetoacetate
-
at pH 8.5, rabbit liver GDH
9.9
acetoacetate
-
at pH 8.5, recombinant rabbit GDH
5.3
L-3-hydroxybutanoate
-
-
14.9
L-3-hydroxybutanoate
-
cofactor NAD+, pH 8.2
22.8
L-3-hydroxybutanoate
-
cofactor NAD+
2.2
L-3-hydroxybutyrate
-
at pH 8.5, recombinant rabbit GDH
2.3
L-3-hydroxybutyrate
-
at pH 8.5, rabbit liver GDH
0.018
L-gulonate
with NAD+, wild-type enzyme, pH 7.0, 25°C
0.18
L-gulonate
-
at pH 8.5, recombinant rabbit GDH
0.21
L-gulonate
-
at pH 8.5, rabbit liver GDH
0.25
L-gulonate
-
cofactor NAD+
0.49
L-gulonate
-
mutant enzyme E157Q, NAD+-linked activity
0.85
L-gulonate
-
cofactor NAD+, pH 8.2
1.3
L-gulonate
with NAD+, mutant enzyme Q41N, pH 7.0, 25°C
1.6
L-gulonate
with NAD+, mutant enzyme E97Q, pH 7.0, 25°C
2.4
L-gulonate
with NADP+, wild-type enzyme, pH 7.0, 25°C
2.6
L-gulonate
with NADP+, mutant enzyme D36R/Q41N, pH 7.0, 25°C
3.3
L-gulonate
with NAD+, mutant enzyme D36R/Q41N, pH 7.0, 25°C
4.4
L-gulonate
-
mutant enzyme S124A, NAD+-linked activity
5.1
L-gulonate
-
cofactor NAD+, pH 8.5
14
L-gulonate
-
mutant enzyme D36R, NAD+-linked activity
14
L-gulonate
with NAD+, mutant enzyme D36R, pH 7.0, 25°C
14
L-gulonate
with NADP+, mutant enzyme Q41N, pH 7.0, 25°C
18
L-gulonate
with NADP+, mutant enzyme D36R, pH 7.0, 25°C
18.5
L-gulonate
-
mutant enzyme D36R, NADP+-linked activity
18.5
L-gulonate
-
mutant enzyme E157Q, NADP+-linked activity
55
L-gulonate
-
cofactor NAD+, pH 8.5
67
L-gulonate
-
cofactor NAD+, pH 7.5
1.2
L-threonate
-
at pH 8.5, recombinant rabbit GDH
2.9
L-threonate
-
at pH 8.5, rabbit liver GDH
0.01
NAD+
wild-type enzyme, pH 7.0, 25°C
0.01
NAD+
-
at pH 8.5, recombinant rabbit GDH
0.011
NAD+
-
at pH 8.5, rabbit liver GDH
0.028
NAD+
mutant enzyme Q41N, pH 7.0, 25°C
0.04
NAD+
-
cosubstrate L-gulonate, pH 8.5
0.054
NAD+
mutant enzyme E97Q, pH 7.0, 25°C
0.09
NAD+
-
cosubstrate L-gulonate, pH 8.2
0.13
NAD+
-
cosubstrate L-gulonate, pH 8.2
1.1
NAD+
-
cosubstrate L-gulonate, pH 7.5 and pH 8.5
1.3
NAD+
mutant enzyme D36R, pH 7.0, 25°C
2.6
NAD+
mutant enzyme D36R/Q41N, pH 7.0, 25°C
0.0005
NADH
-
at pH 8.5, rabbit liver GDH
0.0006
NADH
-
at pH 8.5, recombinant rabbit GDH
0.12
NADP+
mutant enzyme D36R/Q41N, pH 7.0, 25°C
0.2
NADP+
mutant enzyme D36R, pH 7.0, 25°C
0.67
NADP+
wild-type enzyme, pH 7.0, 25°C
0.67
NADP+
-
at pH 8.5, recombinant rabbit GDH
0.86
NADP+
mutant enzyme Q41N, pH 7.0, 25°C
0.89
NADP+
-
at pH 8.5, rabbit liver GDH
additional information
additional information
-
kinetic studies
-
additional information
additional information
-
kinetic studies
-
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
-
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0.733
DL-3-hydroxybutanoate
-
-
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0.34
malonate
Oryctolagus cuniculus
-
reversible inhibition, IC50: 0.34 mM
5.5
malonic acid monoethyl ester
Oryctolagus cuniculus
-
weak inhibition, IC50: 5.5 mM
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0.011
-
in the supernatant
6.71
-
after purification
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6.3
-
reduction of 3-dehydro-L-gulonic acid
9
-
oxidation of L-gulonic acid
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4 - 8
-
reduction of acetoacetate
6.2 - 10
-
oxidation of L-3-hydroxybutanoate
7 - 10
-
oxidation of 3-hydroxybutanoate
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-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
sheep
-
-
brenda
rat
-
-
brenda
-
-
-
brenda
hog
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
Japanese white rabbit
-
-
brenda
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-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
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-
-
brenda
-
-
brenda
-
-
brenda
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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
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CRYL1_BOVIN
321
0
35072
Swiss-Prot
Mitochondrion (Reliability: 5 )
CRYL1_HUMAN
319
0
35419
Swiss-Prot
other Location (Reliability: 5 )
CRYL1_MOUSE
319
0
35209
Swiss-Prot
other Location (Reliability: 4 )
CRYL1_PIG
322
0
35128
Swiss-Prot
other Location (Reliability: 4 )
CRYL1_PONAB
319
0
35437
Swiss-Prot
other Location (Reliability: 5 )
CRYL1_RABIT
319
0
35202
Swiss-Prot
other Location (Reliability: 3 )
CRYL1_RAT
319
0
35341
Swiss-Prot
other Location (Reliability: 4 )
A0A812ASL3_SEPPH
196
3
21886
TrEMBL
Secretory Pathway (Reliability: 1 )
A0A812D5M8_SEPPH
313
1
35442
TrEMBL
Secretory Pathway (Reliability: 5 )
A0A8B6F4L7_MYTGA
318
0
35692
TrEMBL
other Location (Reliability: 3 )
A0A6J8BT44_MYTCO
318
0
35785
TrEMBL
other Location (Reliability: 3 )
A0A6J8C7X7_MYTCO
298
0
33382
TrEMBL
other Location (Reliability: 2 )
A7VMV2_MOUSE
319
0
35209
TrEMBL
other Location (Reliability: 4 )
A0A6J8BSB3_MYTCO
257
0
28639
TrEMBL
other Location (Reliability: 5 )
Q0V973_DANRE
315
0
35096
TrEMBL
other Location (Reliability: 3 )
E3TEE5_ICTPU
255
0
28786
TrEMBL
other Location (Reliability: 2 )
B5X4A9_SALSA
312
0
35029
TrEMBL
Secretory Pathway (Reliability: 2 )
A0A6J8AVR5_MYTCO
154
0
17357
TrEMBL
Mitochondrion (Reliability: 4 )
A0A8B6F451_MYTGA
319
0
35759
TrEMBL
other Location (Reliability: 5 )
A0A6J8CAU5_MYTCO
290
0
32990
TrEMBL
other Location (Reliability: 2 )
Q9R4S4_CLOTY
45
1
4630
TrEMBL
-
B1H3F7_XENTR
319
0
35880
TrEMBL
other Location (Reliability: 2 )
A0A653QGR0_9GAMM
311
0
34672
TrEMBL
-
Q9VXI1_DROME
315
0
34786
TrEMBL
other Location (Reliability: 3 )
A0A6J8ASH8_MYTCO
234
0
26412
TrEMBL
other Location (Reliability: 1 )
A1L2W4_XENLA
319
0
35854
TrEMBL
other Location (Reliability: 2 )
A0A8B6F427_MYTGA
320
0
35890
TrEMBL
Mitochondrion (Reliability: 5 )
A0A8B6BG73_MYTGA
319
0
35538
TrEMBL
other Location (Reliability: 3 )
D6BV38_PIG
322
0
35057
TrEMBL
other Location (Reliability: 4 )
F7SA26_9PROT
312
0
33382
TrEMBL
-
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23500
-
alphabeta, 1 * 23500 + 1 * 40000, SDS-PAGE
40000
-
alphabeta, 1 * 23500 + 1 * 40000, SDS-PAGE
63000
-
sucrose density gradient centrifugation
66000 - 70000
-
33000/unit in vitro, 35000/unit in vivo, SDS-PAGE
36000
-
SDS-PAGE
36000
2 * 36000, recombinant enzyme, SDS-PAGE
36000
-
X-ray diffraction, natural active protein is presumably a dimer 2 * 36000
60000 - 70000
-
HPLC gel filtration
60000 - 70000
-
HPLC gel filtration
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monomer
-
X-ray diffraction, natural active protein is presumably a dimer 2 * 36000
dimer
-
alphabeta, 1 * 23500 + 1 * 40000, SDS-PAGE
dimer
-
alpha2, 2 * 33000-35000, SDS-PAGE
dimer
2 * 36000, recombinant enzyme, SDS-PAGE
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
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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
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D36R/Q41N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E157Q
-
mutation produces no large kinetic alterations
E97Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H145Q
-
inactive enzyme form
N195D
-
inactive enzyme form
N196Q
-
inactive enzyme form
Q41N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S124A
-
mutation decreases the catalytic efficiency 500 fold
D36R
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
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additional information
-
in solution instable, by addition of below mM of cyanide several days in the cold, minor effect through EDTA-addition
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3 M urea results in loss of activity of 83% in 7 min
-
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-18°C, 0.05 M K2HPO4, several weeks, little loss of activity
-
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ammonium sulfate fractionation, Sephadex G-100 column chromatography, Q-Sepharose column chromatography, Blue-Sepharose column chromatography, hydroxylapatite column chromatography
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recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) cells
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expressed in Escherichia coli
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expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) cells
in Escherichia coli strain BL21(DE3)
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medicine
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role in an alternative pathway of the production of xylitol in the lens that causes cataracts in mammalian organisms
medicine
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role in an alternative pathway of the production of xylitol in the lens that causes cataracts in mammalian organisms
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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
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