Literature DB >> 1182101

Sheep liver serine-threonine dehydratase. I. Purification and evidence for covalently linked alpha-ketobutyrate as its cofactor.

G Kapke, L Davis.   

Abstract

L-Serine-threonine dehydratase (EC 4.2.1.16) from sheep liver has been obtained as a highly purified preparation as shown by ultracentrifuge studies and analytical disc gel electrophoresis. The dehydratase has a molecular weight of 98,000 +/- 10,000 and is composed of two nonidentical subunits with molecular weights of 41,000 and 47,000. The 41,000 subunit is covalently linked to the carbonyl reagent-sensitive coenzyme which has been identified as alpha-ketobutyric acid.

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Year:  1975        PMID: 1182101     DOI: 10.1021/bi00690a020

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  2 in total

1.  Role of pyridoxal phosphate in mammalian polyamine biosynthesis. Lack of requirement for mammalian S-adenosylmethionine decarboxylase activity.

Authors:  A E Pegg
Journal:  Biochem J       Date:  1977-07-15       Impact factor: 3.857

2.  Resolution and reconstitution of glutamate decarboxylase from cerebellum.

Authors:  L D Ryan; R Roskoski
Journal:  Neurochem Res       Date:  1976-02       Impact factor: 3.996

  2 in total

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