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Literature summary for 4.1.2.52 extracted from

  • Wang, W.; Baker, P.; Seah, S.Y.
    Comparison of two metal-dependent pyruvate aldolases related by convergent evolution: substrate specificity, kinetic mechanism, and substrate channeling (2010), Biochemistry, 49, 3774-3782.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) 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 Comment 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 Comment 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 Comment Organism Structure
Co2+
-
Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
4-hydroxy-2-oxoheptanedioate = pyruvate + succinate semialdehyde rapid equilibrium random order mechanism Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxobutanoate + acetaldehyde
-
Escherichia coli ?
-
?
pyruvate + acetaldehyde
-
Escherichia coli 4-hydroxy-2-oxopentanoate enzyme lacks stereospecific control producing racemic mixtures of 4-hydroxy-2-oxopentanoate i.e. HOPA ?
pyruvate + butyraldehyde
-
Escherichia coli ?
-
?
pyruvate + DL-glyceraldehyde
-
Escherichia coli ?
-
?
pyruvate + glycolaldehyde
-
Escherichia coli ?
-
?
pyruvate + isobutyraldehyde
-
Escherichia coli ?
-
?
pyruvate + pentaldehyde
-
Escherichia coli ?
-
?
pyruvate + propionaldehyde
-
Escherichia coli ?
-
?
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 ?

Synonyms

Synonyms Comment Organism
HpaI
-
Escherichia coli

Turnover Number [1/s]

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

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment 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