Literature DB >> 30450

Some properties of 3-hydroxy-3-methylglutaryl-coenzyme A synthase from ox liver.

M A Page, P K Tubbs.   

Abstract

Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase (EC 4.1.3.5) was purified from ox liver, and obtained essentially free from 3-oxoacyl-CoA thiolases. The kinetic behaviour, like that of the synthases from chicken liver and yeast, is compatible with a reaction pathway involving condensation of an acetyl-enzyme with acetoacetyl-CoA. The Km for acetoacetyl-CoA, less than 1 micronM at pH 7.8, may possibly be low enough to permit rapid ketogenesis under physiological conditions without the need for a binary complex between the synthase and oxoacyl-CoA thiolase.

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Year:  1978        PMID: 30450      PMCID: PMC1185860          DOI: 10.1042/bj1730925

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  13 in total

1.  Trapping of a novel coenzyme A containing intermediate of 3-hydroxy-3-methylglutaryl-CoA synthase.

Authors:  H M Miziorko; D Shortle; M D Lane
Journal:  Biochem Biophys Res Commun       Date:  1976-03-08       Impact factor: 3.575

2.  The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations.

Authors:  W W CLELAND
Journal:  Biochim Biophys Acta       Date:  1963-01-08

3.  Intracellular localization of the 3-hydroxy-3-methylglutaryl coenzme A cycle enzymes in liver. Separate cytoplasmic and mitochondrial 3-hydroxy-3-methylglutaryl coenzyme A generating systems for cholesterogenesis and ketogenesis.

Authors:  K D Clinkenbeard; W D Reed; R A Mooney; M D Lane
Journal:  J Biol Chem       Date:  1975-04-25       Impact factor: 5.157

4.  Characterization of the different polypeptide components and analysis of subunit assembly in ferritin.

Authors:  K Ishitani; Y Niitsu; I Listowsky
Journal:  J Biol Chem       Date:  1975-04-25       Impact factor: 5.157

5.  On the mechanism of ketogenesis and its control. Purification, kinetic mechanism and regulation of different forms of mitochondrial acetoacetyl-CoA thiolases from ox liver.

Authors:  W Huth; R Jonas; I Wunderlich; W Seubert
Journal:  Eur J Biochem       Date:  1975-11-15

6.  3-Hydroxy-3-methylglutaryl coenzyme A synthase. Evidence for an acetyl-S-enzyme intermediate and identification of a cysteinyl sulfhydryl as the site of acetylation.

Authors:  H M Miziorko; K D Clinkenbeard; W D Reed; M D Lane
Journal:  J Biol Chem       Date:  1975-08-10       Impact factor: 5.157

7.  The kinetic mechanism and properties of the cytoplasmic acetoacetyl-coenzyme A thiolase from rat liver.

Authors:  B Middleton
Journal:  Biochem J       Date:  1974-04       Impact factor: 3.857

8.  The kinetic mechanism of 3-hydroxy-3-methylglutaryl-coenzyme A synthase from baker's yeast.

Authors:  B Middleton
Journal:  Biochem J       Date:  1972-01       Impact factor: 3.857

9.  The purification and some properties of 3-hydroxy-3-methylglutaryl-coenzyme A synthase from Baker's yeast.

Authors:  B Middleton; P K Tubbs
Journal:  Biochem J       Date:  1972-01       Impact factor: 3.857

10.  An enzyme-bound intermediate in the biosynthesis of 3-hydroxy-3-methylglutaryl-coenzyme A.

Authors:  B Middleton; P K Tubbs
Journal:  Biochem J       Date:  1974-01       Impact factor: 3.857

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  3 in total

Review 1.  Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase: a control enzyme in ketogenesis.

Authors:  F G Hegardt
Journal:  Biochem J       Date:  1999-03-15       Impact factor: 3.857

2.  3-Hydroxy-3-methylglutaryl-coenzyme A synthase from ox liver. Properties of its acetyl derivative.

Authors:  D M Lowe; P K Tubbs
Journal:  Biochem J       Date:  1985-04-15       Impact factor: 3.857

3.  3-Hydroxy-3-methylglutaryl-coenzyme A synthase from ox liver. Purification, molecular and catalytic properties.

Authors:  D M Lowe; P K Tubbs
Journal:  Biochem J       Date:  1985-04-15       Impact factor: 3.857

  3 in total

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