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Literature summary for 6.2.1.26 extracted from

  • Bhattacharyya, D.K.; Kwon, O.; Meganathan, R.
    Vitamin K2 (menaquinone) biosynthesis in Escherichia coli: evidence for the presence of an essential histidine residue in o-succinylbenzoyl coenzyme A synthetase (1997), J. Bacteriol., 179, 6061-6065.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
H341A mutant enzyme loses 65% of ist activity and the Km-value for ATP increases 5.4fold Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
diethylpyrocarbonate inactivation follows pseudo-first-order kinetics with a second-order rate constant of 0.00092 /min *microM, partial protection from inactivation by either o-succinylbenzoic acid, ATP, or ATP plus Mg2+ while inactivation is completely prevented by the presence of the combination of ATP, Mg2+ and o-succinylbenzoate Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0735
-
ATP native enzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 2-succinylbenzoate + CoA
-
Escherichia coli AMP + diphosphate + 2-succinylbenzoyl-CoA
-
?
additional information His341 plays an important role in catalysis since it is probably involved in the binding of ATP to the enzyme Escherichia coli ?
-
?