EC Number   |
General Information |
Reference |
|---|
    6.2.1.26 | metabolism |
o-succinylbenzoyl-CoA synthetase, or MenE, is an essential adenylate-forming enzyme in the menaquinone biosynthesis |
-, 745330 |
| 6.2.1.26 | more |
in MenE catalysis, tight gripping interactions of the phosphate-binding loop (P-loop) with the ATP triphosphate moiety and an open-closed conformational change to form a compact adenylation active site create a new binding site for the carboxylate substrate, allowing revelation of the determinants of substrate specificities and in-line alignment of the two substrates for backside nucleophilic substitution reaction by molecular modeling, overview. The ATP-enzyme interaction is suggested to play a crucial catalytic role. positioning and catalytic role of a conserved lysine residue in stabilization of the transition state, molecular docking, overview |
-, 745330 |
| 6.2.1.26 | more |
the basic residue, Arg222, may interact with the aromatic carboxylate of 2-succinylbenzoate |
727306 |
| 6.2.1.26 | physiological function |
ATP-dependent configuration of adenylation active site in o-succinylbenzoyl-CoA synthetase |
-, 745330 |
| 6.2.1.26 | physiological function |
the enzyme is essential in Escherichia coli and is involved in menaquinone biosynthesis |
727306 |
| 6.2.1.26 | physiological function |
the enzyme is essential in Mycobacterium tuberculosis and is involved in menaquinone biosynthesis |
727306 |
| 6.2.1.26 | physiological function |
the enzyme is important in Mycobacterium tuberculosis |
727306 |
