Literature DB >> 1253971

Whither enzyme mechanisms?

J R Knowles.   

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Year:  1976        PMID： 1253971     DOI： 10.1016/0014-5793(76)80854-x

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


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  6 in total

1.  Kinetic parameters of the acyl-enzyme mechanism and conditions for quasi-equilibrium and for optimal catalytic characteristics.

Authors:  K Brocklehurst; C M Topham
Journal:  Biochem J       Date:  1990-09-01       Impact factor: 3.857

2.  Evolution of enzyme catalytic power. Characteristics of optimal catalysis evaluated for the simplest plausible kinetic model.

Authors:  K Brocklehurst
Journal:  Biochem J       Date:  1977-04-01       Impact factor: 3.857

3.  Characterization of the papain active centre by using two-protonic-state electrophiles as reactivity probes. Evidence for nucleophilic reactivity in the un-interrupted cysteine-25-histidine-159 interactive system.

Authors:  M Shipton; K Brochlehurst
Journal:  Biochem J       Date:  1978-05-01       Impact factor: 3.857

4.  The equilibrium assumption is valid for the kinetic treatment of most time-dependent protein-modification reactions.

Authors:  K Brocklehurst
Journal:  Biochem J       Date:  1979-09-01       Impact factor: 3.857

5.  The evolution of enzyme kinetic power.

Authors:  T Keleti; G R Welch
Journal:  Biochem J       Date:  1984-10-15       Impact factor: 3.857

6.  The pre-eminence of k(cat) in the manifestation of optimal enzymic activity delineated by using the Briggs-Haldane two-step irreversible kinetic model.

Authors:  K Brocklehurst; A Cornish-Bowden
Journal:  Biochem J       Date:  1976-10-01       Impact factor: 3.857
  6 in total

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