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Identification of six important amino acid residues of MenA from Bacillus subtilis natto for enzyme activity and formation of menaquinone.

Enzyme and microbial technology - 1 Aug 2020

Hu Liu-Xiu, Feng Jing-Jing, Wu Jing, Li Wei, Gningue Sokhna Mbacke, Yang Zi-Ming, Wang Zhou, Liu Yan, Xue Zheng-Lian

Abstract excerpt

The enzyme 1, 4-dihydroxy-2-naphthoic acid (DHNA) prenyltransferase (MenA) is a critical player in determining the eﬃciency of the menaquinone (MK) synthesis pathway and is an attractive target for the development of novel chemotherapeutics against pathogenic Gram-positive bacteria. However, there has been no report on structural properties or active region of MenA. To solve this challenge, we predicted the...

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PMID: 32527527
DOI: 10.1016/j.enzmictec.2020.109583

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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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