Literature DB >> 7018582

Purification and some properties of L-glycol dehydrogenase from hen's muscle.

A Bernardo, J Burgos, R Martín.   

Abstract

1. An enzyme which catalyzes the NAD(P)H-linked reversible reduction of uncharged vicinal dicarbonyls and alpha-hydroxycarbonyls to L-(+)-glycols has been purified from hen's muscle. This enzyme has not been previously described. 2. According to the rules of the I.U.P.A.C.-I.U.B. Enzymes Commission, the systematic name of L-(+)-glycol:NAD(P) oxidoreductase and the trivial name of L-glycol dehydrogenase are proposed for the enzyme. 3. Three forms of this enzyme differing in pI have been isolated; two forms, which together represent about 90% of total recovered activity, and electrophoretically pure. 4. Molecular weight, pH profiles and affinity for substrates are also described.

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Year:  1981        PMID: 7018582     DOI: 10.1016/0005-2744(81)90283-7

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  1 in total

1.  Purification and characterization of diacetyl-reducing enzymes from Staphylococcus aureus.

Authors:  I Vidal; J González; A Bernardo; R Martín
Journal:  Biochem J       Date:  1988-04-15       Impact factor: 3.857

  1 in total

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