Literature DB >> 3545209

Pyruvate decarboxylase--potentially inactive in the absence of the substrate.

G Hübner, A Schellenberger.   

Abstract

Using two independent methods, it was shown that pyruvate decarboxylase of brewer's yeast/EC 4.1.1.1./showing a sigmoidal v/S-shape and a corresponding activation phase in the product formation is potentially inactive in the absence of its substrate-pyruvate.

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Year:  1986        PMID: 3545209

Source DB:  PubMed          Journal:  Biochem Int        ISSN: 0158-5231


  3 in total

1.  Covalently bound substrate at the regulatory site of yeast pyruvate decarboxylases triggers allosteric enzyme activation.

Authors:  Steffen Kutter; Manfred S Weiss; Georg Wille; Ralph Golbik; Michael Spinka; Stephan König
Journal:  J Biol Chem       Date:  2009-02-26       Impact factor: 5.157

2.  The influence of the effectors of yeast pyruvate decarboxylase (PDC) on the conformation of the dimers and tetramers and their pH-dependent equilibrium.

Authors:  S König; D Svergun; M H Koch; G Hübner; A Schellenberger
Journal:  Eur Biophys J       Date:  1993       Impact factor: 1.733

3.  The influence of protein concentration on oligomer structure and catalytic function of two pyruvate decarboxylases.

Authors:  Steffen Kutter; Michael Spinka; Michel H J Koch; Stephan König
Journal:  Protein J       Date:  2007-12       Impact factor: 2.371

  3 in total

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