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show all sequences of 4.1.2.52

Crystal structure of reaction intermediates in pyruvate class II aldolase: substrate cleavage, enolate stabilization, and substrate specificity

Coincon, M.; Wang, W.; Sygusch, J.; Seah, S.Y.; J. Biol. Chem. 287, 36208-36221 (2012)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
in complex with substrate or products, hanging drop vapor diffusion method, using
Escherichia coli
Engineering
Amino acid exchange
Commentary
Organism
D42A
inactive, the mutation leads to a concomitant loss of the metal ion
Escherichia coli
H45A
the mutation leads to a decrease in kcat of the enzyme by 78fold
Escherichia coli
H45Q
the mutation leads to a decrease in kcat of the enzyme by 2059fold
Escherichia coli
R70A
almost inactive
Escherichia coli
R70K
the mutation reduces catalytic efficiency by 270fold
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.05
-
2-oxo-3-methyl-4-hydroxypentanoate
wild type enzyme, at pH 8.0 and 25°C
Escherichia coli
0.35
-
4-hydroxy-2-oxoheptane-1,7-dioate
using H2O as solvent, in the presence of 0.5 mM Co2+, at pH 8.0 and 25°C
Escherichia coli
0.38
-
(S)-4-hydroxy-2-oxopentanoate
wild type enzyme, with 0.5 mM Co2+, at pH 8.0 and 25°C
Escherichia coli
3.32
-
(S)-4-hydroxy-2-oxopentanoate
mutant enzyme R70K, with 0.5 mM Co2+, at pH 8.0 and 25°C
Escherichia coli
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
required
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4-hydroxy-2-oxoheptane-1,7-dioate
Escherichia coli
-
pyruvate + succinate semialdehyde
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
B1IS70
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-4-hydroxy-2-oxopentanoate
-
725493
Escherichia coli
?
-
-
-
?
2-oxo-3-methyl-4-hydroxypentanoate
efficient substrate
725493
Escherichia coli
2-oxobutyrate + acetaldehyde
-
-
-
?
4-hydroxy-2-oxoheptane-1,7-dioate
-
725493
Escherichia coli
pyruvate + succinate semialdehyde
-
-
-
?
Subunits
Subunits
Commentary
Organism
trimer of dimers
x-ray crystallography
Escherichia coli
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
11.8
-
(S)-4-hydroxy-2-oxopentanoate
mutant enzyme R70K, with 0.5 mM Co2+, at pH 8.0 and 25°C
Escherichia coli
14
-
2-oxo-3-methyl-4-hydroxypentanoate
wild type enzyme, at pH 8.0 and 25°C
Escherichia coli
353.5
-
(S)-4-hydroxy-2-oxopentanoate
wild type enzyme, with 0.5 mM Co2+, at pH 8.0 and 25°C
Escherichia coli
361.5
-
4-hydroxy-2-oxoheptane-1,7-dioate
using H2O as solvent, in the presence of 0.5 mM Co2+, at pH 8.0 and 25°C
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
in complex with substrate or products, hanging drop vapor diffusion method, using
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D42A
inactive, the mutation leads to a concomitant loss of the metal ion
Escherichia coli
H45A
the mutation leads to a decrease in kcat of the enzyme by 78fold
Escherichia coli
H45Q
the mutation leads to a decrease in kcat of the enzyme by 2059fold
Escherichia coli
R70A
almost inactive
Escherichia coli
R70K
the mutation reduces catalytic efficiency by 270fold
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.05
-
2-oxo-3-methyl-4-hydroxypentanoate
wild type enzyme, at pH 8.0 and 25°C
Escherichia coli
0.35
-
4-hydroxy-2-oxoheptane-1,7-dioate
using H2O as solvent, in the presence of 0.5 mM Co2+, at pH 8.0 and 25°C
Escherichia coli
0.38
-
(S)-4-hydroxy-2-oxopentanoate
wild type enzyme, with 0.5 mM Co2+, at pH 8.0 and 25°C
Escherichia coli
3.32
-
(S)-4-hydroxy-2-oxopentanoate
mutant enzyme R70K, with 0.5 mM Co2+, at pH 8.0 and 25°C
Escherichia coli
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
required
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4-hydroxy-2-oxoheptane-1,7-dioate
Escherichia coli
-
pyruvate + succinate semialdehyde
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-4-hydroxy-2-oxopentanoate
-
725493
Escherichia coli
?
-
-
-
?
2-oxo-3-methyl-4-hydroxypentanoate
efficient substrate
725493
Escherichia coli
2-oxobutyrate + acetaldehyde
-
-
-
?
4-hydroxy-2-oxoheptane-1,7-dioate
-
725493
Escherichia coli
pyruvate + succinate semialdehyde
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
trimer of dimers
x-ray crystallography
Escherichia coli
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
11.8
-
(S)-4-hydroxy-2-oxopentanoate
mutant enzyme R70K, with 0.5 mM Co2+, at pH 8.0 and 25°C
Escherichia coli
14
-
2-oxo-3-methyl-4-hydroxypentanoate
wild type enzyme, at pH 8.0 and 25°C
Escherichia coli
353.5
-
(S)-4-hydroxy-2-oxopentanoate
wild type enzyme, with 0.5 mM Co2+, at pH 8.0 and 25°C
Escherichia coli
361.5
-
4-hydroxy-2-oxoheptane-1,7-dioate
using H2O as solvent, in the presence of 0.5 mM Co2+, at 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
3.55
-
(S)-4-hydroxy-2-oxopentanoate
mutant enzyme R70K, with 0.5 mM Co2+, at pH 8.0 and 25°C
Escherichia coli
941
-
(S)-4-hydroxy-2-oxopentanoate
wild type enzyme, with 0.5 mM Co2+, at pH 8.0 and 25°C
Escherichia coli
1000
-
4-hydroxy-2-oxoheptane-1,7-dioate
using H2O as solvent, in the presence of 0.5 mM Co2+, at 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
3.55
-
(S)-4-hydroxy-2-oxopentanoate
mutant enzyme R70K, with 0.5 mM Co2+, at pH 8.0 and 25°C
Escherichia coli
941
-
(S)-4-hydroxy-2-oxopentanoate
wild type enzyme, with 0.5 mM Co2+, at pH 8.0 and 25°C
Escherichia coli
1000
-
4-hydroxy-2-oxoheptane-1,7-dioate
using H2O as solvent, in the presence of 0.5 mM Co2+, at 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
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
1
-
-
-
-
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