Exploiting the high-resolution crystal structure of Staphylococcus aureus MenH to gain insight into enzyme activity.

ABSTRACT:

Background

MenH (2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase) is a key enzyme in the biosynthesis of menaquinone, catalyzing an unusual 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate.

Results

The crystal structure of Staphylococcus aureus MenH has been determined at 2 Å resolution. In the absence of a complex to inform on aspects of specificity a model of the enzyme-substrate complex has been used in conjunction with previously published kinetic analyses, site-directed mutagenesis studies and comparisons with orthologues to investigate the structure and reactivity of MenH.

Conclusions

The overall basic active site displays pronounced hydrophobic character on one side and these properties complement

SUBMITTER: Dawson A 

PROVIDER: S-EPMC3097144 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature