Literature DB >> 205413

Investigation on the kinetic mechanism of octopine dehydrogenase. A regulatory behavior.

M O Monneuse-Doublet, A Olomucki, J Buc.   

Abstract

The kinetic scheme of octopine dehydrogenase of Pecten maximus L., a monomeric enzyme obeying a bi-ter sequential mechanism, was completed, essentially in the forward reaction, by steady-state studies over a wide range of substrate concentration at pH 7.0. Deviation from the Michaelis-Menten behavior with respect to NAD+ and other significant kinetic data led us to ascribe for octopine dehydrogenase mechanism the mnemonical enzyme concept. In addition, another regulatory behavior can be envisaged involving the formation of two dead-end complexes enzyme.NADH.D-octopine and enzyme.NAD+.pyruvate.L-arginine.

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Year:  1978        PMID: 205413     DOI: 10.1111/j.1432-1033.1978.tb12185.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  4 in total

1.  Kinetics and mechanism of action of aldehyde reductase from pig kidney.

Authors:  W S Davidson; T G Flynn
Journal:  Biochem J       Date:  1979-02-01       Impact factor: 3.857

2.  Patterns of apparent co-operativity in a simple random non-equilibrium enzyme--substrate--modifier mechanism. Comparison with equilibrium allosteric models.

Authors:  E P Whitehead; M R Egmond
Journal:  Biochem J       Date:  1979-02-01       Impact factor: 3.857

3.  Generalized microscopic reversibility, kinetic co-operativity of enzymes and evolution.

Authors:  J Ricard
Journal:  Biochem J       Date:  1978-12-01       Impact factor: 3.857

Review 4.  Cooperativity in monomeric enzymes with single ligand-binding sites.

Authors:  Carol M Porter; Brian G Miller
Journal:  Bioorg Chem       Date:  2011-11-17       Impact factor: 5.275

  4 in total

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