Literature DB >> 7150236

A quick method for the determination of inhibition constants.

S G Waley.   

Abstract

The inhibition constant Ki in the common case of competitive inhibition can be obtained by simple comparison of progress curves in the presence and in the absence of inhibitor. The difference between the times taken for the concentration of substrate to fall to the same value is used to obtain Ki. The procedure to use when the product inhibits is described. When there is mixed inhibition, reactions at different substrate concentrations are used to obtain both inhibition constants.

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Year:  1982        PMID: 7150236      PMCID: PMC1158531          DOI: 10.1042/bj2050631

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


  6 in total

1.  The use of the direct linear plot for determining initial velocities.

Authors:  A Cornish-Bowden
Journal:  Biochem J       Date:  1975-08       Impact factor: 3.857

2.  Enzymic parameters: measurement of V and Km.

Authors:  H J Lee; I B Wilson
Journal:  Biochim Biophys Acta       Date:  1971-09-22

3.  Use of integrated rate equations in estimating the kinetic constants of enzyme-catalyzed reactions.

Authors:  G W Schwert
Journal:  J Biol Chem       Date:  1969-03-10       Impact factor: 5.157

4.  Half-time analysis of the integrated Michaelis equation. Simulation and use of the half-time plot and its direct linear variant in the analysis of some alpha-chymotrypsin, papain- and fumarase-catalysed reactions.

Authors:  C W Wharton; R J Szawelski
Journal:  Biochem J       Date:  1982-05-01       Impact factor: 3.857

5.  Kinetic analysis of progress curves.

Authors:  B A Orsi; K F Tipton
Journal:  Methods Enzymol       Date:  1979       Impact factor: 1.600

6.  Reversible inhibitors of penicillinases.

Authors:  P A Kiener; S G Waley
Journal:  Biochem J       Date:  1978-01-01       Impact factor: 3.857

  6 in total
  18 in total

1.  Progress-curve equations for reversible enzyme-catalysed reactions inhibited by tight-binding inhibitors.

Authors:  S E Szedlacsek; V Ostafe; R G Duggleby; M Serban; M O Vlad
Journal:  Biochem J       Date:  1990-02-01       Impact factor: 3.857

2.  Syntheses and Biological Evaluations of Highly Functionalized Hydroxamate Containing and N-Methylthio Monobactams as Anti-Tuberculosis and β-Lactamase Inhibitory Agents.

Authors:  Mark W Majewski; Kyle D Watson; Sanghyun Cho; Patricia A Miller; Scott G Franzblau; Marvin J Miller
Journal:  Medchemcomm       Date:  2015-10-05       Impact factor: 3.597

3.  Antibacterial Spectrum of a Tetrazole-Based Reversible Inhibitor of Serine β-Lactamases.

Authors:  Orville A Pemberton; Xiujun Zhang; Derek A Nichols; Kyle DeFrees; Priyadarshini Jaishankar; Richard Bonnet; Jessie Adams; Lindsey N Shaw; Adam R Renslo; Yu Chen
Journal:  Antimicrob Agents Chemother       Date:  2018-07-27       Impact factor: 5.191

4.  The determination of specificity constants in enzyme-catalysed reactions.

Authors:  I E Crompton; S G Waley
Journal:  Biochem J       Date:  1986-10-01       Impact factor: 3.857

5.  Structure-based optimization of a non-beta-lactam lead results in inhibitors that do not up-regulate beta-lactamase expression in cell culture.

Authors:  Donatella Tondi; Federica Morandi; Richard Bonnet; M Paola Costi; Brian K Shoichet
Journal:  J Am Chem Soc       Date:  2005-04-06       Impact factor: 15.419

6.  Kinetic parameters from progress curves of competing substrates. Application to beta-lactamases.

Authors:  S G Waley
Journal:  Biochem J       Date:  1983-05-01       Impact factor: 3.857

7.  Imipenem as substrate and inhibitor of beta-lactamases.

Authors:  J Monks; S G Waley
Journal:  Biochem J       Date:  1988-07-15       Impact factor: 3.857

8.  Structure-based optimization of cephalothin-analogue boronic acids as beta-lactamase inhibitors.

Authors:  Stefania Morandi; Federica Morandi; Emilia Caselli; Brian K Shoichet; Fabio Prati
Journal:  Bioorg Med Chem       Date:  2007-11-07       Impact factor: 3.641

9.  Syntheses and studies of new forms of N-sulfonyloxy β-lactams as potential antibacterial agents and β-lactamase inhibitors.

Authors:  Serena Carosso; Marvin J Miller
Journal:  Bioorg Med Chem       Date:  2015-08-14       Impact factor: 3.641

10.  Characterization of cell-bound papain-soluble beta-lactamases in BRO-1 and BRO-2 producing strains of Moraxella (Branhamella) catarrhalis and Moraxella nonliquefaciens.

Authors:  I Eliasson; C Kamme; M Vang; S G Waley
Journal:  Eur J Clin Microbiol Infect Dis       Date:  1992-04       Impact factor: 3.267

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