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Literature summary for 4.1.2.52 extracted from

  • Coincon, M.; Wang, W.; Sygusch, J.; Seah, S.Y.
    Crystal structure of reaction intermediates in pyruvate class II aldolase: substrate cleavage, enolate stabilization, and substrate specificity (2012), J. Biol. Chem., 287, 36208-36221.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.2.52

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with substrate or products, hanging drop vapor diffusion method, using Escherichia coli

Protein Variants

Protein Variants Comment 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 Comment 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 Comment Organism Structure
Co2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-hydroxy-2-oxoheptane-1,7-dioate Escherichia coli
-
 pyruvate + succinate semialdehyde
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli B1IS70
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-4-hydroxy-2-oxopentanoate
-
 Escherichia coli ?
-
 ?
2-oxo-3-methyl-4-hydroxypentanoate efficient substrate Escherichia coli 2-oxobutyrate + acetaldehyde
-
 ?
4-hydroxy-2-oxoheptane-1,7-dioate
-
 Escherichia coli pyruvate + succinate semialdehyde
-
 ?

Subunits

Subunits Comment Organism
trimer of dimers x-ray crystallography Escherichia coli

Synonyms

Synonyms Comment Organism
HpaI
-
 Escherichia coli
HpcH
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment 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 Comment 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