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Article

Dynamics of catalysis revealed from the crystal structures of mutants of diaminopimelate epimerase.

Biochemical and biophysical research communications - 23 Nov 2007

Pillai Bindu, Cherney Maia, Diaper Christopher M, Sutherland Andrew, Blanchard John S, Vederas John C, James Michael N G

Abstract excerpt

Diaminopimelate (DAP) epimerase catalyzes the stereoinversion of ll-DAP to meso-DAP, a precursor of l-lysine and an essential component of the bacterial peptidoglycan. This function is vital to bacteria and the enzyme therefore represents an attractive target for the design of novel anti-bacterials. DAP epimerase belongs to the group of PLP-independent amino acid racemases that function through a rather unusual...

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Source

Identifiers

PMID: 17889830
DOI: 10.1016/j.bbrc.2007.09.012

Genes

DAP

Variants

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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