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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1981-12-15
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pubmed:abstractText |
An NAD-linked acetoacetyl-CoA reductase of Zoolgoea ramigera I-16-M was purified to electrophoretic homogeneity. In contrast to the D(-)-3-hydroxybutyryl-CoA-specific NADP-linked acetoacetyl-CoA reductase from the same bacterium [Saito, T. et al (1977) Arch. Microbiol. 114, 211 - 217], the purified enzyme was strictly stereospecific to L(+)-3-hydroxybutyryl-CoA, and was active not only with NAD+ but also with NADP+, although NADP+ was less effective than NAD+ as coenzyme. The enzyme showed a pH optimum at 6.3 for the reduction of acetoacetyl-CoA and at 8.0 for the oxidation of L(+)-3-hydroxybutyryl-CoA. In the reduction reaction, Km values for acetoacetyl-Coa and NADH were 8.8 microM and 6.5 microM, respectively, and in the oxidation reaction, Km values for L(+)-3-hydroxybutyryl-CoA and DNA+ were 7.0 microM and 32 microM, respectively. Among various 3-hydroxyacyl-CoAs tested, L(+)-3-hydroxybutyryl-CoA and L(+)-3-hydroxyvaleryl-CoA were the most active substrates. Poly(3-hydroxybutyrate) synthesis from acetyl-CoA, by a system reconstituted from purified preparations of 3-oxothiolase, acetoacetyl-CoA reductase and poly(3-hydroxybutyrate) synthase, was observed when the NADP-linked but not the NAD-linked reductase was used. These findings indicate that the NAD-linked acetoacetyl-CoA reductase is not directly involved in the biosynthesis of poly(3-hydroxybutyrate).
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetoacetates,
http://linkedlifedata.com/resource/pubmed/chemical/Acyl Coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/Alcohol Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/NAD,
http://linkedlifedata.com/resource/pubmed/chemical/acetoacetyl-CoA reductase
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
118
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
53-9
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:7026239-Acetoacetates,
pubmed-meshheading:7026239-Acyl Coenzyme A,
pubmed-meshheading:7026239-Alcohol Oxidoreductases,
pubmed-meshheading:7026239-Kinetics,
pubmed-meshheading:7026239-Molecular Weight,
pubmed-meshheading:7026239-NAD,
pubmed-meshheading:7026239-Substrate Specificity,
pubmed-meshheading:7026239-Zoogloea
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pubmed:year |
1981
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pubmed:articleTitle |
An NAD-linked acetoacetyl-CoA reductase from Zoogloea ramigera I-16-M.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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