Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.2.4.1 extracted from

  • Balakrishnan, A.; Nemeria, N.S.; Chakraborty, S.; Kakalis, L.; Jordan, F.
    Determination of pre-steady-state rate constants on the Escherichia coli pyruvate dehydrogenase complex reveals that loop movement controls the rate-limiting step (2012), J. Am. Chem. Soc., 134, 18644-18655.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
D549A in the mutant, binding and reductive acetylation of E2p lipoyl domains are highly impaired Escherichia coli
E401K in the mutant, binding and reductive acetylation of E2p lipoyl domains are highly impaired Escherichia coli
H407A in the mutant, binding and reductive acetylation of E2p lipoyl domains are highly impaired Escherichia coli
Y177A in the mutant, binding and reductive acetylation of E2p lipoyl domains are highly impaired Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.73
-
E2p lipoyl domain wild type enzyme, at pH 7.0 and 30°C Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
99474
-
x * 99474, calculated from amino acid sequence Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + E2p lipoyl domain
-
Escherichia coli acetylated E2p lipoyl domain + CO2
-
?

Subunits

Subunits Comment Organism
? x * 99474, calculated from amino acid sequence Escherichia coli

Synonyms

Synonyms Comment Organism
E1p
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.08
-
E2p lipoyl domain mutant enzyme H407A, at pH 7.0 and 30°C Escherichia coli
0.7
-
E2p lipoyl domain mutant enzyme D549A, at pH 7.0 and 30°C Escherichia coli
0.83
-
E2p lipoyl domain mutant enzyme E401K, at pH 7.0 and 30°C Escherichia coli
3.31
-
E2p lipoyl domain mutant enzyme Y177A, at pH 7.0 and 30°C Escherichia coli
95
-
E2p lipoyl domain wild type enzyme, at pH 7.0 and 30°C Escherichia coli

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate dependent on Escherichia coli