Methylobacterium rhodesianum MB 126 possesses two acetoacetyl-CoA reductases View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-03

AUTHORS

Gisela Mothes, Wolfgang Babel

ABSTRACT

Two constitutive acetoacetyl-CoA (AcAc-CoA) reductases were purified from Methylobacterium rhodesianum MB 126, an NADPH-linked d(-)-β-hydroxybutyryl-CoA forming reductase (enzyme A) and an NADH-and NADPH-linked l(+)-β-hydroxybutyryl-CoA forming reductase (enzyme B). Enzyme A and B give apparent Km values of 15 μM and 30 μM for AcAc-CoA, 18 μM for NADPH and 30 μM for NADH, respectively. They are inhibited by AcAc-CoA at concentrations higher than 25 μM and 50 μM, respectively. The contribution of the two reductases to poly-β-hydroxybutyrate synthesis is discussed. More... »

PAGES

277-280

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00248705

DOI

http://dx.doi.org/10.1007/bf00248705

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1007396397


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