BRENDA - Enzyme Database show
show all sequences of 1.1.1.45

Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase

Ishikura, S.; Usami, N.; Araki, M.; Hara, A.; J. Biochem. 137, 303-314 (2005)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli
Oryctolagus cuniculus
Engineering
Amino acid exchange
Commentary
Organism
D36R
mutation leads to a switch in the favor of NADP(H) specificity, suggesting an important role of Asp36 in the coenzyme specificity
Oryctolagus cuniculus
E157Q
mutation produces no large kinetic alterations
Oryctolagus cuniculus
H145Q
inactive enzyme form
Oryctolagus cuniculus
N195D
inactive enzyme form
Oryctolagus cuniculus
N196Q
inactive enzyme form
Oryctolagus cuniculus
S124A
mutation decreases the catalytic efficiency 500 fold
Oryctolagus cuniculus
Inhibitors
Inhibitors
Commentary
Organism
Structure
Cibacron blue
competitive inhibition with respect to NAD+
Oryctolagus cuniculus
malonate
reversible inhibition, IC50: 0.34 mM
Oryctolagus cuniculus
malonic acid monoethyl ester
weak inhibition, IC50: 5.5 mM
Oryctolagus cuniculus
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
Oryctolagus cuniculus
p-Chloromercuriphenylsulfonate
0.001 mM, complete inhibition
Oryctolagus cuniculus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
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
Oryctolagus cuniculus
0.0005
-
NADH
at pH 8.5, rabbit liver GDH
Oryctolagus cuniculus
0.0006
-
NADH
at pH 8.5, recombinant rabbit GDH
Oryctolagus cuniculus
0.01
-
NAD+
at pH 8.5, recombinant rabbit GDH
Oryctolagus cuniculus
0.011
-
NAD+
at pH 8.5, rabbit liver GDH
Oryctolagus cuniculus
0.18
-
L-gulonate
at pH 8.5, recombinant rabbit GDH
Oryctolagus cuniculus
0.21
-
L-gulonate
at pH 8.5, rabbit liver GDH
Oryctolagus cuniculus
0.49
-
L-gulonate
mutant enzyme E157Q, NAD+-linked activity
Oryctolagus cuniculus
0.67
-
NADP+
at pH 8.5, recombinant rabbit GDH
Oryctolagus cuniculus
0.89
-
NADP+
at pH 8.5, rabbit liver GDH
Oryctolagus cuniculus
1.2
-
L-threonate
at pH 8.5, recombinant rabbit GDH
Oryctolagus cuniculus
2.2
-
L-3-hydroxybutyrate
at pH 8.5, recombinant rabbit GDH
Oryctolagus cuniculus
2.3
-
L-3-hydroxybutyrate
at pH 8.5, rabbit liver GDH
Oryctolagus cuniculus
2.9
-
L-threonate
at pH 8.5, rabbit liver GDH
Oryctolagus cuniculus
4.4
-
L-gulonate
mutant enzyme S124A, NAD+-linked activity
Oryctolagus cuniculus
8.3
-
acetoacetate
at pH 8.5, rabbit liver GDH
Oryctolagus cuniculus
9.9
-
acetoacetate
at pH 8.5, recombinant rabbit GDH
Oryctolagus cuniculus
14
-
L-gulonate
mutant enzyme D36R, NAD+-linked activity
Oryctolagus cuniculus
18.5
-
L-gulonate
mutant enzyme D36R, NADP+-linked activity; mutant enzyme E157Q, NADP+-linked activity
Oryctolagus cuniculus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Oryctolagus cuniculus
5829
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35000
-
2 * 35000
Oryctolagus cuniculus
36000
-
SDS-PAGE
Oryctolagus cuniculus
70000
-
gel filtration
Oryctolagus cuniculus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Oryctolagus cuniculus
-
Japanese white rabbit
-
Purification (Commentary)
Commentary
Organism
ammonium sulfate fractionation, Sephadex G-100 column chromatography, Q-Sepharose column chromatography, Blue-Sepharose column chromatography, hydroxylapatite column chromatography
Oryctolagus cuniculus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
lens
-
Oryctolagus cuniculus
-
liver
-
Oryctolagus cuniculus
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.011
-
in the supernatant
Oryctolagus cuniculus
6.71
-
after purification
Oryctolagus cuniculus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
? + NADP+
-
669147
Oryctolagus cuniculus
? + NADPH
-
-
-
?
acetoacetate + NADH
-
669147
Oryctolagus cuniculus
? + NAD+
-
-
-
?
L-3-hydroxybutyrate + ?
-
669147
Oryctolagus cuniculus
?
-
-
-
?
L-gulonate + NAD+
-
669147
Oryctolagus cuniculus
3-dehydro-L-gulonate + NADH + H+
-
-
-
?
L-threonate + ?
-
669147
Oryctolagus cuniculus
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
2 * 35000
Oryctolagus cuniculus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
-
Oryctolagus cuniculus
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
-
Oryctolagus cuniculus
NADP+
-
Oryctolagus cuniculus
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Oryctolagus cuniculus
-
-
7.3
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.34
-
reversible inhibition, IC50: 0.34 mM
Oryctolagus cuniculus
malonate
5.5
-
weak inhibition, IC50: 5.5 mM
Oryctolagus cuniculus
malonic acid monoethyl ester
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli
Oryctolagus cuniculus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
-
Oryctolagus cuniculus
NADP+
-
Oryctolagus cuniculus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D36R
mutation leads to a switch in the favor of NADP(H) specificity, suggesting an important role of Asp36 in the coenzyme specificity
Oryctolagus cuniculus
E157Q
mutation produces no large kinetic alterations
Oryctolagus cuniculus
H145Q
inactive enzyme form
Oryctolagus cuniculus
N195D
inactive enzyme form
Oryctolagus cuniculus
N196Q
inactive enzyme form
Oryctolagus cuniculus
S124A
mutation decreases the catalytic efficiency 500 fold
Oryctolagus cuniculus
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.34
-
reversible inhibition, IC50: 0.34 mM
Oryctolagus cuniculus
malonate
5.5
-
weak inhibition, IC50: 5.5 mM
Oryctolagus cuniculus
malonic acid monoethyl ester
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Cibacron blue
competitive inhibition with respect to NAD+
Oryctolagus cuniculus
malonate
reversible inhibition, IC50: 0.34 mM
Oryctolagus cuniculus
malonic acid monoethyl ester
weak inhibition, IC50: 5.5 mM
Oryctolagus cuniculus
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
Oryctolagus cuniculus
p-Chloromercuriphenylsulfonate
0.001 mM, complete inhibition
Oryctolagus cuniculus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
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
Oryctolagus cuniculus
0.0005
-
NADH
at pH 8.5, rabbit liver GDH
Oryctolagus cuniculus
0.0006
-
NADH
at pH 8.5, recombinant rabbit GDH
Oryctolagus cuniculus
0.01
-
NAD+
at pH 8.5, recombinant rabbit GDH
Oryctolagus cuniculus
0.011
-
NAD+
at pH 8.5, rabbit liver GDH
Oryctolagus cuniculus
0.18
-
L-gulonate
at pH 8.5, recombinant rabbit GDH
Oryctolagus cuniculus
0.21
-
L-gulonate
at pH 8.5, rabbit liver GDH
Oryctolagus cuniculus
0.49
-
L-gulonate
mutant enzyme E157Q, NAD+-linked activity
Oryctolagus cuniculus
0.67
-
NADP+
at pH 8.5, recombinant rabbit GDH
Oryctolagus cuniculus
0.89
-
NADP+
at pH 8.5, rabbit liver GDH
Oryctolagus cuniculus
1.2
-
L-threonate
at pH 8.5, recombinant rabbit GDH
Oryctolagus cuniculus
2.2
-
L-3-hydroxybutyrate
at pH 8.5, recombinant rabbit GDH
Oryctolagus cuniculus
2.3
-
L-3-hydroxybutyrate
at pH 8.5, rabbit liver GDH
Oryctolagus cuniculus
2.9
-
L-threonate
at pH 8.5, rabbit liver GDH
Oryctolagus cuniculus
4.4
-
L-gulonate
mutant enzyme S124A, NAD+-linked activity
Oryctolagus cuniculus
8.3
-
acetoacetate
at pH 8.5, rabbit liver GDH
Oryctolagus cuniculus
9.9
-
acetoacetate
at pH 8.5, recombinant rabbit GDH
Oryctolagus cuniculus
14
-
L-gulonate
mutant enzyme D36R, NAD+-linked activity
Oryctolagus cuniculus
18.5
-
L-gulonate
mutant enzyme D36R, NADP+-linked activity; mutant enzyme E157Q, NADP+-linked activity
Oryctolagus cuniculus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Oryctolagus cuniculus
5829
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35000
-
2 * 35000
Oryctolagus cuniculus
36000
-
SDS-PAGE
Oryctolagus cuniculus
70000
-
gel filtration
Oryctolagus cuniculus
Purification (Commentary) (protein specific)
Commentary
Organism
ammonium sulfate fractionation, Sephadex G-100 column chromatography, Q-Sepharose column chromatography, Blue-Sepharose column chromatography, hydroxylapatite column chromatography
Oryctolagus cuniculus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
lens
-
Oryctolagus cuniculus
-
liver
-
Oryctolagus cuniculus
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.011
-
in the supernatant
Oryctolagus cuniculus
6.71
-
after purification
Oryctolagus cuniculus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
? + NADP+
-
669147
Oryctolagus cuniculus
? + NADPH
-
-
-
?
acetoacetate + NADH
-
669147
Oryctolagus cuniculus
? + NAD+
-
-
-
?
L-3-hydroxybutyrate + ?
-
669147
Oryctolagus cuniculus
?
-
-
-
?
L-gulonate + NAD+
-
669147
Oryctolagus cuniculus
3-dehydro-L-gulonate + NADH + H+
-
-
-
?
L-threonate + ?
-
669147
Oryctolagus cuniculus
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 35000
Oryctolagus cuniculus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
-
Oryctolagus cuniculus
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Oryctolagus cuniculus
-
-
7.3
Other publictions for EC 1.1.1.45
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
712765
Asada
Dimeric crystal structure of r ...
Oryctolagus cuniculus
J. Mol. Biol.
401
906-920
2010
-
-
1
1
4
-
-
17
-
-
1
1
-
2
-
-
1
1
-
2
-
-
4
2
1
-
-
-
1
-
-
4
-
-
-
-
-
1
4
1
4
-
-
-
-
17
-
-
1
1
-
-
-
1
-
2
-
-
4
2
1
-
-
-
1
-
-
-
-
1
1
-
-
-
695345
Asada
Crystallization and preliminar ...
Oryctolagus cuniculus
Acta Crystallogr. Sect. F
64
228-230
2008
-
-
1
1
-
-
-
-
-
-
1
-
-
2
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
669147
Ishikura
Structural and functional char ...
Oryctolagus cuniculus
J. Biochem.
137
303-314
2005
-
-
1
-
6
-
5
19
1
-
3
-
-
3
-
-
1
-
-
2
2
-
5
1
-
-
-
-
1
-
-
2
-
1
2
-
-
1
2
-
6
-
2
5
-
19
1
-
3
-
-
-
-
1
-
2
2
-
5
1
-
-
-
-
1
-
-
1
-
-
-
-
-
-
286146
Goode
Accumulation of xylitol in the ...
Bos taurus, Rattus norvegicus
FEBS Lett.
395
174-178
1996
-
2
-
-
-
-
-
-
-
-
2
2
-
2
-
-
-
-
-
2
-
-
4
-
-
-
-
-
-
-
-
4
-
-
-
-
2
-
4
-
-
-
-
-
-
-
-
-
2
2
-
-
-
-
-
2
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286911
Menotti-Raymond
Further characterization of L- ...
Drosophila melanogaster
Biochim. Biophys. Acta
841
15-21
1985
-
-
-
-
-
-
-
-
-
-
1
1
-
3
-
1
1
-
-
-
2
-
2
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
1
1
-
-
1
1
-
-
2
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286910
Cannistraro
Subunit structure and kinetic ...
Drosophila melanogaster
Biochim. Biophys. Acta
569
1-5
1979
-
-
-
-
-
1
2
4
-
-
3
1
-
2
-
-
-
-
-
-
1
-
3
1
-
-
-
2
1
-
-
3
-
-
-
-
-
-
3
-
-
1
-
2
-
4
-
-
3
1
-
-
-
-
-
-
1
-
3
1
-
-
-
2
1
-
-
-
-
-
-
-
-
-
286909
Borack
-
Organ distribution of Drosophi ...
Drosophila melanogaster
Experientia
30
31
1974
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
4
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
4
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286908
Koundakjian
3-Hydroxy acid dehydrogenases ...
Ovis aries
Biochem. J.
127
449-452
1972
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
4
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
4
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286907
Borack
Drosophila beta-L-hydroxy acid ...
Drosophila melanogaster
J. Biol. Chem.
246
5345-5350
1970
-
-
-
-
-
-
-
3
-
-
1
1
-
1
-
-
1
-
-
-
1
-
4
-
-
-
-
-
1
1
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
3
-
-
1
1
-
-
-
1
-
-
1
-
4
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
286906
Dworsky
-
L-3-Aldonic acid dehydrogenase ...
Schwanniomyces occidentalis
Acta Biochim. Pol.
9
269-277
1964
-
-
-
-
-
-
3
4
-
-
-
1
-
1
-
-
1
-
-
-
-
-
5
-
-
-
1
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
3
-
4
-
-
-
1
-
-
-
1
-
-
-
-
5
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
286905
Smiley
-
Purification and properties of ...
Sus scrofa
J. Biol. Chem.
236
357-364
1961
1
-
-
-
-
-
2
8
1
1
-
1
-
1
-
-
1
-
-
1
-
1
16
-
-
-
-
-
2
2
-
2
-
-
-
1
-
-
2
-
-
-
-
2
-
8
1
1
-
1
-
-
-
1
-
1
-
1
16
-
-
-
-
-
2
2
-
-
-
-
-
-
-
-