O-succinylbenzoate—CoA ligase
| o-succinylbenzoate-CoA ligase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 6.2.1.26 | ||||||
| CAS number | 72506-70-8 | ||||||
| Databases | |||||||
| IntEnz | IntEnz view | ||||||
| BRENDA | BRENDA entry | ||||||
| ExPASy | NiceZyme view | ||||||
| KEGG | KEGG entry | ||||||
| MetaCyc | metabolic pathway | ||||||
| PRIAM | profile | ||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||
| Gene Ontology | AmiGO / EGO | ||||||
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In enzymology, an o-succinylbenzoate-CoA ligase (EC 6.2.1.26) is an enzyme that catalyzes the chemical reaction
- ATP + o-succinylbenzoate + CoA
AMP + diphosphate + o-succinylbenzoyl-CoA
The 3 substrates of this enzyme are ATP, o-succinylbenzoate, and CoA, whereas its 3 products are AMP, diphosphate, and o-succinylbenzoyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is 2-succinylbenzoate:CoA ligase (AMP-forming). Other names in common use include 2-succinylbenzoyl-coenzyme A synthetase, and 2-succinylbenzoate:CoA ligase (AMP-forming). This enzyme participates in ubiquinone biosynthesis.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2OKT and 2OLA.
References
- Heide L, Arendt S, Leistner E (1982). "Enzymatic synthesis, characterization, and metabolism of the coenzyme A ester of o-succinylbenzoic acid, an intermediate in menaquinone (vitamin K2) biosynthesis". J. Biol. Chem. 257 (13): 7396–400. PMID 7045104.
- Kolkmann R, Leistner E (1987). "4-(2'-Carboxyphenyl)-4-oxobutyryl coenzyme A ester, an intermediate in vitamin K2 (menaquinone) biosynthesis". Z. Naturforsch. [C]. 42 (11-12): 1207–14. PMID 2966501.
- Meganathan R, Bentley R (1979). "Menaquinone (vitamin K2) biosynthesis: conversion of o-succinylbenzoic acid to 1,4-dihydroxy-2-naphthoic acid by Mycobacterium phlei enzymes". J. Bacteriol. 140 (1): 92–8. PMC 216783. PMID 500558. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=216783.