Observation of thiamin-bound intermediates and microscopic rate constants for their interconversion on 1-deoxy-D-xylulose 5-phosphate synthase: 600-fold rate acceleration of pyruvate decarboxylation by D-glyceraldehyde-3-phosphate

The thiamin diphosphate (ThDP)-dependent enzyme 1-deoxy-D-xylulose 5-phosphate (DXP) synthase carries out the condensation of pyruvate as 2-hydroxyethyl donor with D-glyceraldehyde-3-phosphate (D-GAP) as acceptor forming DXP. Toward understanding catalysis of this potential anti-infective drug targe...

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Auteurs principaux: Patel, Hetalben, Nemeria, Natalia S., Brammer, Leighanne A., Freel Meyers, Caren L., Jordan, Frank
Format: Artigo
Langue:Inglês
Publié: 2012
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Article
Accès en ligne:https://ncbi.nlm.nih.gov/pmc/articles/PMC3494461/
https://ncbi.nlm.nih.gov/pubmed/23072514
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/ja307315u
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