Defining critical residues for substrate binding to 1-deoxy-d-xylulose 5-phosphate synthase: Active site substitutions stabilize the pre-decarboxylation intermediate C2α-lactylthiamin diphosphate

1-Deoxy-d-xylulose 5-phosphate (DXP) synthase catalyzes formation of DXP from pyruvate and d-glyceraldehyde 3-phosphate (d-GAP) in a thiamin diphosphate (ThDP)-dependent manner, and is the first step in the essential pathway to isoprenoids in human pathogens. Understanding the mechanism of this uniq...

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Autores principales: Basta, Leighanne A. Brammer, Patel, Hetalben, Kakalis, Lazaros, Jordan, Frank, Meyers, Caren L. Freel
Formato: Artigo
Lenguaje:Inglês
Publicado: 2014
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Article
Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC4065394/
https://ncbi.nlm.nih.gov/pubmed/24767541
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1111/febs.12823
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