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Article

How essential is the 'essential' active-site lysine in dihydrodipicolinate synthase?

Biochimie - 1 Jul 2010

Soares da Costa Tatiana P, Muscroft-Taylor Andrew C, Dobson Renwick C J, Devenish Sean R A, Jameson Geoffrey B, Gerrard Juliet A

Abstract excerpt

Dihydrodipicolinate synthase (DHDPS, E.C. 4.2.1.52), a validated antibiotic target, catalyses the first committed step in the lysine biosynthetic pathway: the condensation reaction between (S)-aspartate beta-semialdehyde [(S)-ASA] and pyruvate via the formation of a Schiff base intermediate between pyruvate and the absolutely conserved active-site lysine. Escherichia coli DHDPS mutants K161A and K161R of the...

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PMID: 20353808
DOI: 10.1016/j.biochi.2010.03.004

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

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