Scientists reveal distinct substrate-binding mode in o-succinylbenzoyl-CoA synthetase

Using a catalytically competent Bacillus subtilis mutant protein complexed with an OSB-CoA analogue, researchers from the Hong Kong University of Science and Technology revealed a thioesterification active site conserved among MenE orthologues and a substrate-binding mode distinct from those of many other acyl/aryl-CoA synthetases. Several residues that specifically contribute to the thioesterification half-reaction without affecting the adenylation half-reaction were identified, and they observed a substantial movement of the activated succinyl group in the thioesterification half-reaction.

Scientists reveal distinct substrate-binding mode in o-succinylbenzoyl-CoA synthetase

o-Succinylbenzoyl-CoA (OSB-CoA) synthetase (MenE) is an essential enzyme in bacterial vitamin K biosynthesis and an important target in the development of new antibiotics. It is a member of ...

Wed 13 Sep 17 from Phys.org

Scientists reveal distinct substrate-binding mode in o-succinylbenzoyl-CoA synthetase, Wed 13 Sep 17 from Eurekalert

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