Formation of D-3-hydroxybutyryl-coenzyme A by an acetoacetyl-coenzyme A reductase in Syntrophomonas wolfei subsp. wolfei
- Univ. of Oklahoma, Norman, OK (United States). Dept. of Botany and Microbiology
Cell-free extracts of Syntrophomonas wolfei subsp. wolfei synthesized D-({minus})-3-hydroxybutyryl-coenzyme A (CoA) (the stereoisomer required for the synthesis of poly-{beta}-hydroxyalkanoate) from acetoacetyl-CoA, but not crotonyl-CoA, and NAD(P)H. Ammonium sulfate fractionation and ion exchange chromatography separated an acetoacetyl-CoA reductase activity that formed D-({minus})-3-hydroxybutyryl-CoA from the {beta}-oxidation enzyme activity, L-(+)-3-hydroxyacyl-CoA dehydrogenase. The former activity was further purified by hydroxylapatite and affinity chromatography. The most pure acetoacetyl-CoA reductase preparations formed D-({minus})-3-hydroxybutyryl-CoA from acetoacetyl-CoA and had high specific activity using either NADH or NADPH as the electron donor. Thus, S. wolfei makes D-({minus})-3-hydroxybutyryl-CoA by an acetoacetyl-CoA reductase rather than by a D-isomer specific enoyl-CoA hydratase and the reducing equivalents required for PHA synthesis from acetoacetyl-CoA can be supplied from the NADH made during {beta}-oxidation.
- Sponsoring Organization:
- USDOE, Washington, DC (United States)
- DOE Contract Number:
- FG05-89ER14003
- OSTI ID:
- 514560
- Journal Information:
- Archives of Microbiology, Journal Name: Archives of Microbiology Vol. 159; ISSN 0302-8933; ISSN AMICCW
- Country of Publication:
- United States
- Language:
- English
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