Proton-Nuclear Magnetic Resonance Analyses of the Substrate Specificity of a β-Ketolase from Pseudomonas putida, Acetopyruvate Hydrolase

A revised purification of acetopyruvate hydrolase from orcinol-grown Pseudomonas putida ORC is described. This carbon-carbon bond hydrolase, which is the last inducible enzyme of the orcinol catabolic pathway, is monomeric with a molecular size of ∼38 kDa; it hydrolyzes acetopyruvate to equimolar qu...

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Библиографические подробности

Опубликовано в::	J Bacteriol
Главные авторы:	Pokorny, Diana, Brecker, Lothar, Pogorevc, Mateja, Steiner, Walter, Griengl, Herfried, Kappe, Thomas, Ribbons, Douglas W.
Формат:	Artigo
Язык:	Inglês
Опубликовано:	American Society for Microbiology (ASM) 1999
Предметы:	Enzymes and Proteins
Online-ссылка:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC93995/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10438778/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.181.16.5051-5059.1999
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