BRENDA - Enzyme Database show
show all sequences of 1.1.1.185

L-Glycol dehydrogenase from hen muscle

Burgos, J.; Sarmiento, R.M.; Methods Enzymol. 89, 523-526 (1982)

Data extracted from this reference:

General Stability
General Stability
Organism
easily inactivated in high molarity buffers
Gallus gallus
very stable in both water and low molarity buffers of pH 7 at 0-4C
Gallus gallus
Inhibitors
Inhibitors
Commentary
Organism
Structure
acetone
pI 7.2 form
Gallus gallus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Gallus gallus
-
hen
-
Purification (Commentary)
Commentary
Organism
3 enzyme forms: pI 7.2, pI 6.2 and pI 4.8
Gallus gallus
Reaction
Reaction
Commentary
Organism
an L-glycol + NAD(P)+ = a 2-hydroxycarbonyl compound + NAD(P)H + H+
glyoxal reduction by enzyme form pI 7.2 follows ordered bi-bi mechanism in which the coenzyme is the first substrate to bind to the enzyme
Gallus gallus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
muscle
-
Gallus gallus
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.4
-
-
Gallus gallus
Storage Stability
Storage Stability
Organism
-18C, enzyme at any stage of purification
Gallus gallus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
R1-CO-CHOH-R2 + NAD(P)H
-
286135
Gallus gallus
R1-CHOH-CHOH-R2 + NAD(P)+
-
-
-
r
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Gallus gallus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
6.6
-
Gallus gallus
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
7
-
very stable in both water and low molarity buffers of pH 7 at 0-4C
Gallus gallus
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Gallus gallus
NADH
-
Gallus gallus
NADPH
-
Gallus gallus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Gallus gallus
NADH
-
Gallus gallus
NADPH
-
Gallus gallus
General Stability (protein specific)
General Stability
Organism
easily inactivated in high molarity buffers
Gallus gallus
very stable in both water and low molarity buffers of pH 7 at 0-4C
Gallus gallus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
acetone
pI 7.2 form
Gallus gallus
Purification (Commentary) (protein specific)
Commentary
Organism
3 enzyme forms: pI 7.2, pI 6.2 and pI 4.8
Gallus gallus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
muscle
-
Gallus gallus
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.4
-
-
Gallus gallus
Storage Stability (protein specific)
Storage Stability
Organism
-18C, enzyme at any stage of purification
Gallus gallus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
R1-CO-CHOH-R2 + NAD(P)H
-
286135
Gallus gallus
R1-CHOH-CHOH-R2 + NAD(P)+
-
-
-
r
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Gallus gallus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
6.6
-
Gallus gallus
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
7
-
very stable in both water and low molarity buffers of pH 7 at 0-4C
Gallus gallus
Other publictions for EC 1.1.1.185
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)
286137
Carballo
Kinetics of alpha-dicarbonyls ...
Enterobacter aerogenes
Ital. J. Biochem.
42
79-89
1993
-
-
-
-
-
-
3
8
-
-
-
-
-
2
-
-
-
1
-
-
-
-
7
-
1
-
-
-
1
-
-
2
-
-
-
-
-
-
2
-
-
-
-
3
-
8
-
-
-
-
-
-
-
-
-
-
-
-
7
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
286136
Prieto
Kinetics of alpha-dicarbonyls ...
Gallus gallus
Arch. Biochem. Biophys.
224
372-377
1983
-
-
-
-
-
-
1
8
-
-
-
-
-
1
-
-
1
1
-
1
-
-
5
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
1
-
8
-
-
-
-
-
-
-
1
-
1
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286135
Burgos
L-Glycol dehydrogenase from he ...
Gallus gallus
Methods Enzymol.
89
523-526
1982
-
-
-
-
-
2
1
-
-
-
-
-
-
1
-
-
1
1
-
1
1
1
1
-
1
-
-
-
1
-
1
3
-
-
-
-
-
-
3
-
-
2
-
1
-
-
-
-
-
-
-
-
-
1
-
1
1
1
1
-
1
-
-
-
1
-
1
-
-
-
-
-
-
-
286134
Bernardo
Purification and some properti ...
Gallus gallus
Biochim. Biophys. Acta
659
189-198
1981
-
-
-
-
-
2
-
17
-
-
1
-
-
1
-
-
1
-
-
1
1
1
10
-
1
-
-
-
1
-
1
4
-
-
-
-
-
-
4
-
-
2
-
-
-
17
-
-
1
-
-
-
-
1
-
1
1
1
10
-
1
-
-
-
1
-
1
-
-
-
-
-
-
-