EC Number |
Title |
Organism |
---|
6.2.1.26 | Structural basis for the ATP-dependent configuration of adenylation active site in Bacillus subtilis o-succinylbenzoyl-CoA synthetase |
Bacillus subtilis |
6.2.1.26 | Structural basis for the ATP-dependent configuration of adenylation active site in Bacillus subtilis o-succinylbenzoyl-CoA synthetase |
Bacillus subtilis 168 |
6.2.1.26 | 4-(2'-Carboxyphenyl)-4-oxobutyryl coenzyme A ester, an intermediate in vitamin K2 (menaquinone) biosynthesis |
Escherichia coli |
6.2.1.26 | 4-(2'-Carboxyphenyl)-4-oxobutyryl coenzyme A ester, an intermediate in vitamin K2 (menaquinone) biosynthesis |
Mycolicibacterium phlei |
6.2.1.26 | Bacillus anthracis o-succinylbenzoyl-CoA synthetase: reaction kinetics and a novel inhibitor mimicking its reaction intermediate |
Bacillus anthracis |
6.2.1.26 | Enzymatic synthesis of the coenzyme A ester of o-succinylbenzoic acid, an intermediate in menaquinone (vitamin K2) biosynthesis |
Mycolicibacterium phlei |
6.2.1.26 | Enzymatic synthesis, characterization, and metabolism of the coenzyme A ester of o-succinylbenzoic acid, an intermediate in menaquinone (vitamin K2) biosynthesis |
Mycolicibacterium phlei |
6.2.1.26 | Menaquinone (vitamin K2) biosynthesis: conversion of o-succinylbenzoic acid to 1,4-dihydroxy-2-naphthoic acid by Mycobacterium phlei enzymes |
Mycolicibacterium phlei |
6.2.1.26 | Menaquinone (vitamin K2) biosynthesis: overexpression, purification, and properties of o-succinylbenzoyl-coenzyme A synthetase from Escherichia coli |
Escherichia coli |
6.2.1.26 | O-Succinylbenzoate:coenzyme A ligase, an enzyme involved in menaquinone (vitamin K2) biosynthesis displays braod specificity |
Mycolicibacterium phlei |