Literature DB >> 1212215

A quenched-flow study of the reaction catalysed by creatine kinase.

Y Engelborghs, A Marsh, H Gutfreund.   

Abstract

The reaction catalysed by creatine kinase was studied in both directions by quenched-flow techniques to follow the initial product formation in the millisecond range. In both directions the amount of product formed increases linearly with time, and the turnover number corresponds to the steady-state value. Extrapolation to zero time indicates the absence of either a large transient phase or a large lag phase in both directions. This indicates that the actual chemical reaction is rate-limiting, and that all possible isomerizations before or after the chemical step must be much more rapid.

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Year:  1975        PMID: 1212215      PMCID: PMC1172323          DOI: 10.1042/bj1510047

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


  7 in total

1.  Approaches to the study of enzyme mechanisms lactate dehydrogenase.

Authors:  J J. Holbrook; H Gutfreund
Journal:  FEBS Lett       Date:  1973-04-15       Impact factor: 4.124

2.  Adenosinetriphosphate-creatine transphosphorylase. I. Isolation of the crystalline enzyme from rabbit muscle.

Authors:  S A KUBY; L NODA; H A LARDY
Journal:  J Biol Chem       Date:  1954-07       Impact factor: 5.157

3.  Relaxation spectra of adenosine triphosphate-creatine phosphotransferase.

Authors:  G G Hammes; J K Hurst
Journal:  Biochemistry       Date:  1969-03       Impact factor: 3.162

4.  A simple method for the preparation of 32-P-labelled adenosine triphosphate of high specific activity.

Authors:  I M Glynn; J B Chappell
Journal:  Biochem J       Date:  1964-01       Impact factor: 3.857

5.  Isotope exchange studies of the mechanism of the reaction catalyzed by adenosine triphosphate: creatine phosphotransferase.

Authors:  J F Morrison; W W Cleland
Journal:  J Biol Chem       Date:  1966-02-10       Impact factor: 5.157

6.  The mechanism of the reaction catalysed by adenosine triphosphate-creatine phosphotransferase.

Authors:  J F Morrison; E James
Journal:  Biochem J       Date:  1965-10       Impact factor: 3.857

7.  The reversibility of adenosine triphosphate cleavage by myosin.

Authors:  C R Bagshaw; D R Trentham
Journal:  Biochem J       Date:  1973-06       Impact factor: 3.857

  7 in total
  2 in total

1.  Expression, purification from inclusion bodies, and crystal characterization of a transition state analog complex of arginine kinase: a model for studying phosphagen kinases.

Authors:  G Zhou; G Parthasarathy; T Somasundaram; A Ables; L Roy; S J Strong; W R Ellington; M S Chapman
Journal:  Protein Sci       Date:  1997-02       Impact factor: 6.725

2.  Cryobaroenzymic studies as a tool for investigating activated complexes: creatine kinase.ADP.Mg.nitrate.creatine as a model.

Authors:  C Balny; F Travers; T Barman; P Douzou
Journal:  Proc Natl Acad Sci U S A       Date:  1985-11       Impact factor: 11.205

  2 in total

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