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Article

Structural analysis reveals the substrate-binding mechanism for the expanded substrate specificity of mutant meso-diaminopimelate dehydrogenase.

Chembiochem : a European journal of chemical biology - 13 Apr 2015

Liu Weidong, Guo Rey-Ting, Chen Xi, Li Zhe, Gao Xiuzhen, Huang Chun-Hsiang, Wu Qiaqing, Feng Jinhui, Zhu Dunming

Abstract excerpt

A meso-diaminopimelate dehydrogenase (DAPDH) from Clostridium tetani E88 (CtDAPDH) was found to have low activity toward the D-amino acids other than its native substrate. Site-directed mutagenesis similar to that carried out on the residues mutated by Vedha-Peters et al. resulted in a mutant enzyme with highly improved catalytic ability for the synthesis of D-amino acids. The crystal structures of the CtDAPDH...

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PMID: 25754803
DOI: 10.1002/cbic.201402632

Genes

DAP

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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