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show all sequences of 4.1.2.52

Comparison of two metal-dependent pyruvate aldolases related by convergent evolution: substrate specificity, kinetic mechanism, and substrate channeling

Wang, W.; Baker, P.; Seah, S.Y.; Biochemistry 49, 3774-3782 (2010)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
the active site of HpaI is formed by approx. 30 residues from adjacent dimers and consists of an approx. 15 A deep bell-shaped cleft with an approx. 12 A wide mouth. This broad entrance to the active site is predominantly lined with noncharged residues and a few positively charged residues
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
2-oxobutanoate
competitive inhibition
Escherichia coli
2-Oxopentanoate
competitive inhibition
Escherichia coli
4-methyl-2-oxopentanoate
competitive inhibition
Escherichia coli
glyoxylate
competitive inhibition
Escherichia coli
pyruvate
; competitive inhibition
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
5.6
-
pyruvate
steady-state kinetic parameter, pH 8.0 and 25°C
Escherichia coli
9.1
-
Succinic semialdehyde
Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
13.4
-
Butyraldehyde
Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
32.9
-
propionaldehyde
Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
33.3
-
glycolaldehyde
Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
50.1
-
acetaldehyde
Km(app) with 2-oxobutanoate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
62.1
-
acetaldehyde
steady-state kinetic parameter, pH 8.0 and 25°C
Escherichia coli
62.9
-
acetaldehyde
Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
73.8
-
Isobutyraldehyde
Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
88.6
-
DL-glyceraldehyde
Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
-
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
pyruvate + succinic semialdehyde
Escherichia coli
-
4-hydroxy-2-oxo-1,7-heptanedioate
enzyme lacks stereospecific control producing racemic mixtures of its physiological substrate, 4-hydroxy-2-oxo-1,7-heptanedioate
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Reaction
Reaction
Commentary
Organism
4-hydroxy-2-oxoheptanedioate = pyruvate + succinate semialdehyde
rapid equilibrium random order mechanism
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-oxobutanoate + acetaldehyde
-
702377
Escherichia coli
?
-
-
-
?
pyruvate + acetaldehyde
-
702377
Escherichia coli
4-hydroxy-2-oxopentanoate
enzyme lacks stereospecific control producing racemic mixtures of 4-hydroxy-2-oxopentanoate i.e. HOPA
-
-
?
pyruvate + butyraldehyde
-
702377
Escherichia coli
?
-
-
-
?
pyruvate + DL-glyceraldehyde
-
702377
Escherichia coli
?
-
-
-
?
pyruvate + glycolaldehyde
-
702377
Escherichia coli
?
-
-
-
?
pyruvate + isobutyraldehyde
-
702377
Escherichia coli
?
-
-
-
?
pyruvate + pentaldehyde
-
702377
Escherichia coli
?
-
-
-
?
pyruvate + propionaldehyde
-
702377
Escherichia coli
?
-
-
-
?
pyruvate + succinic semialdehyde
-
702377
Escherichia coli
4-hydroxy-2-oxo-1,7-heptanedioate
enzyme lacks stereospecific control producing racemic mixtures of its physiological substrate, 4-hydroxy-2-oxo-1,7-heptanedioate
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
5.6
-
DL-glyceraldehyde
Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
21.9
-
acetaldehyde
Kcat(app) with 2-oxobutanoate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
64.9
-
Isobutyraldehyde
Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
132.5
-
Butyraldehyde
Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
175.5
-
glycolaldehyde
Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
203.8
-
Succinic semialdehyde
Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
205.4
-
acetaldehyde
Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
219.5
-
pyruvate
steady-state kinetic parameter, with acetaldehyde as aldehyde donor, pH 8.0 and 25°C
Escherichia coli
358.4
-
propionaldehyde
Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.4
-
glyoxylate
pH 8.0, 25°C
Escherichia coli
0.5
-
2-oxobutanoate
pH 8.0, 25°C
Escherichia coli
0.51
-
pyruvate
pH 8.0, 25°C
Escherichia coli
2.01
-
pyruvate
pH 8.0, 25°C
Escherichia coli
3.6
-
2-Oxopentanoate
pH 8.0, 25°C
Escherichia coli
6.98
-
4-methyl-2-oxopentanoate
pH 8.0, 25°C
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
the active site of HpaI is formed by approx. 30 residues from adjacent dimers and consists of an approx. 15 A deep bell-shaped cleft with an approx. 12 A wide mouth. This broad entrance to the active site is predominantly lined with noncharged residues and a few positively charged residues
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2-oxobutanoate
competitive inhibition
Escherichia coli
2-Oxopentanoate
competitive inhibition
Escherichia coli
4-methyl-2-oxopentanoate
competitive inhibition
Escherichia coli
glyoxylate
competitive inhibition
Escherichia coli
pyruvate
; competitive inhibition
Escherichia coli
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.4
-
glyoxylate
pH 8.0, 25°C
Escherichia coli
0.5
-
2-oxobutanoate
pH 8.0, 25°C
Escherichia coli
0.51
-
pyruvate
pH 8.0, 25°C
Escherichia coli
2.01
-
pyruvate
pH 8.0, 25°C
Escherichia coli
3.6
-
2-Oxopentanoate
pH 8.0, 25°C
Escherichia coli
6.98
-
4-methyl-2-oxopentanoate
pH 8.0, 25°C
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
5.6
-
pyruvate
steady-state kinetic parameter, pH 8.0 and 25°C
Escherichia coli
9.1
-
Succinic semialdehyde
Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
13.4
-
Butyraldehyde
Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
32.9
-
propionaldehyde
Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
33.3
-
glycolaldehyde
Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
50.1
-
acetaldehyde
Km(app) with 2-oxobutanoate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
62.1
-
acetaldehyde
steady-state kinetic parameter, pH 8.0 and 25°C
Escherichia coli
62.9
-
acetaldehyde
Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
73.8
-
Isobutyraldehyde
Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
88.6
-
DL-glyceraldehyde
Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
-
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
pyruvate + succinic semialdehyde
Escherichia coli
-
4-hydroxy-2-oxo-1,7-heptanedioate
enzyme lacks stereospecific control producing racemic mixtures of its physiological substrate, 4-hydroxy-2-oxo-1,7-heptanedioate
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-oxobutanoate + acetaldehyde
-
702377
Escherichia coli
?
-
-
-
?
pyruvate + acetaldehyde
-
702377
Escherichia coli
4-hydroxy-2-oxopentanoate
enzyme lacks stereospecific control producing racemic mixtures of 4-hydroxy-2-oxopentanoate i.e. HOPA
-
-
?
pyruvate + butyraldehyde
-
702377
Escherichia coli
?
-
-
-
?
pyruvate + DL-glyceraldehyde
-
702377
Escherichia coli
?
-
-
-
?
pyruvate + glycolaldehyde
-
702377
Escherichia coli
?
-
-
-
?
pyruvate + isobutyraldehyde
-
702377
Escherichia coli
?
-
-
-
?
pyruvate + pentaldehyde
-
702377
Escherichia coli
?
-
-
-
?
pyruvate + propionaldehyde
-
702377
Escherichia coli
?
-
-
-
?
pyruvate + succinic semialdehyde
-
702377
Escherichia coli
4-hydroxy-2-oxo-1,7-heptanedioate
enzyme lacks stereospecific control producing racemic mixtures of its physiological substrate, 4-hydroxy-2-oxo-1,7-heptanedioate
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
5.6
-
DL-glyceraldehyde
Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
21.9
-
acetaldehyde
Kcat(app) with 2-oxobutanoate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
64.9
-
Isobutyraldehyde
Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
132.5
-
Butyraldehyde
Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
175.5
-
glycolaldehyde
Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
203.8
-
Succinic semialdehyde
Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
205.4
-
acetaldehyde
Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
219.5
-
pyruvate
steady-state kinetic parameter, with acetaldehyde as aldehyde donor, pH 8.0 and 25°C
Escherichia coli
358.4
-
propionaldehyde
Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.063
-
DL-glyceraldehyde
Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
0.4
-
acetaldehyde
Kcat/Km(app) with 2-oxobutanoate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
0.9
-
Isobutyraldehyde
Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
3.3
-
acetaldehyde
Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
5.27
-
glycolaldehyde
Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
9.9
-
Butyraldehyde
Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
10.9
-
propionaldehyde
Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
20
-
pentaldehyde
Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
22.2
-
Succinic semialdehyde
Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.063
-
DL-glyceraldehyde
Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
0.4
-
acetaldehyde
Kcat/Km(app) with 2-oxobutanoate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
0.9
-
Isobutyraldehyde
Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
3.3
-
acetaldehyde
Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
5.27
-
glycolaldehyde
Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
9.9
-
Butyraldehyde
Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
10.9
-
propionaldehyde
Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
20
-
pentaldehyde
Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
22.2
-
Succinic semialdehyde
Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C
Escherichia coli
Other publictions for EC 4.1.2.52
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)
725493
Coincon
Crystal structure of reaction ...
Escherichia coli
J. Biol. Chem.
287
36208-36221
2012
-
-
-
1
5
-
-
4
-
1
-
1
-
1
-
-
-
-
-
-
-
-
3
1
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
1
5
-
-
-
-
4
-
1
-
1
-
-
-
-
-
-
-
-
3
1
-
-
-
4
-
-
-
-
-
-
-
-
3
3
702377
Wang
Comparison of two metal-depend ...
Escherichia coli
Biochemistry
49
3774-3782
2010
-
-
-
1
-
-
5
10
-
1
-
1
-
1
-
-
-
1
-
-
-
-
9
-
-
-
-
9
-
-
-
-
6
-
-
-
-
-
-
1
-
-
-
5
6
10
-
1
-
1
-
-
-
-
-
-
-
-
9
-
-
-
-
9
-
-
-
-
-
-
-
-
9
9
722258
Wang
The role of a conserved histid ...
Escherichia coli
FEBS Lett.
582
3385-3388
2008
-
-
1
-
2
1
-
4
-
1
1
-
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
3
-
1
-
-
-
-
-
-
-
1
-
-
2
1
-
-
-
4
-
1
1
-
-
-
-
1
-
-
-
-
1
-
-
-
-
3
-
1
-
-
-
-
-
-
3
3
722955
Rea
Structure and mechanism of Hpc ...
Escherichia coli
J. Mol. Biol.
373
866-876
2007
-
-
1
1
-
-
-
-
-
-
1
1
-
2
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
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-
-
-
-
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-
1
-
1
-
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-
-
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-
1
1
-
-
-
1
-
-
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-
1
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
721601
Wang
Purification and biochemical c ...
Escherichia coli
Biochemistry
44
9447-9455
2005
-
-
1
-
1
-
2
6
-
9
1
1
-
1
-
-
1
-
-
-
-
-
5
-
-
-
-
3
-
-
-
-
2
-
-
-
-
1
-
-
1
-
-
2
2
6
-
9
1
1
-
-
-
1
-
-
-
-
5
-
-
-
-
3
-
-
-
-
-
1
1
-
3
3