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Article

Activation of thiamine diphosphate in pyruvate decarboxylase from Zymomonas mobilis.

FEBS letters - 28 Dec 1998

Tittmann K, Mesch K, Pohl M, Hübner G

Abstract excerpt

Replacement of tryptophan 392 located in the active site cavity of pyruvate decarboxylase (PDC; EC 4.1.1.1) from Zymomonas mobilis by methionine or glutamine yields enzymes with smaller catalytic constants of 8.5 s(-1) and 3.6 s(-1) at 4 degrees C, compared to that of the wild-type enzyme (17 s(-1)). The rate constants of the H/D exchange at the C2 of the coenzyme thiamine diphosphate have been determined to be...

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Identifiers

PMID: 9891980
DOI: 10.1016/s0014-5793(98)01594-4

Genes

PDC

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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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