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 K m 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.
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Mothes, G., Babel, W. Methylobacterium rhodesianum MB 126 possesses two acetoacetyl-CoA reductases. Arch. Microbiol. 161, 277–280 (1994). https://doi.org/10.1007/BF00248705
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DOI: https://doi.org/10.1007/BF00248705