BRENDA - Enzyme Database show
show all sequences of 2.7.1.165

Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli

Hubbard, B.K.; Koch, M.; Palmer, D.R.J.; Babbitt, P.C.; Gerlt, J.A.; Biochemistry 37, 14369-14375 (1998)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.051
-
(R)-glycerate
pH 7.5, 22°C
Escherichia coli
0.061
-
ATP
pH 7.5, 22°C
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + (R)-glycerate
Escherichia coli
enzymes in the (D)-glucarate/galactarate catabolic pathway
ADP + 2-phospho-(R)-glycerate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + (R)-glycerate
-
5083
Escherichia coli
ADP + 2-phospho-(R)-glycerate
-
-
-
?
ATP + (R)-glycerate
enzymes in the (D)-glucarate/galactarate catabolic pathway
5083
Escherichia coli
ADP + 2-phospho-(R)-glycerate
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at
Escherichia coli
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.5
-
ATP
pH 7.5, 22°C
Escherichia coli
2.5
-
(R)-glycerate
pH 7.5, 22°C
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.051
-
(R)-glycerate
pH 7.5, 22°C
Escherichia coli
0.061
-
ATP
pH 7.5, 22°C
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + (R)-glycerate
Escherichia coli
enzymes in the (D)-glucarate/galactarate catabolic pathway
ADP + 2-phospho-(R)-glycerate
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + (R)-glycerate
-
5083
Escherichia coli
ADP + 2-phospho-(R)-glycerate
-
-
-
?
ATP + (R)-glycerate
enzymes in the (D)-glucarate/galactarate catabolic pathway
5083
Escherichia coli
ADP + 2-phospho-(R)-glycerate
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at
Escherichia coli
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.5
-
ATP
pH 7.5, 22°C
Escherichia coli
2.5
-
(R)-glycerate
pH 7.5, 22°C
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Escherichia coli
Other publictions for EC 2.7.1.165
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)
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1
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1
1
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696906
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1937-1941
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1
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1
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686769
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3025-3028
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672800
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1
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2
1
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5
-
4
-
14
6
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5
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1
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1
13
2
2
2
2
3
2
1
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685823
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3
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6
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1
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7
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1
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2
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1
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3
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2
1
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1
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7
1
1
1
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2
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2
4
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2
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1
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1
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4
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5
7
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2
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3
3
5
2
4
2
4
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2
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4
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2
2
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1
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1
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1
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699594
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Reed, G.H.: Method for the enz ...
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32
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1
1
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2
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1
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1
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5083
Hubbard
Evolution of enzymatic activit ...
Escherichia coli
Biochemistry
37
14369-14375
1998
-
-
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-
-
-
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2
-
-
-
1
-
1
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2
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1
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1
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1
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1
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2
1
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641338
Yoshida
Purification and characterizat ...
Hyphomicrobium methylovorum
Eur. J. Biochem.
210
849-854
1992
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8
1
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6
2
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1
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1
1
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641336
Hill
The purification of glycerate ...
Hyphomicrobium sp., Pseudomonas sp.
J. Gen. Microbiol.
83
187-190
1974
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