Literature DB >> 1930157

The kinetics of substrate-induced inactivation.

S G Waley1.   

Abstract

The kinetics of a branched-pathway mechanism for a simple enzymic reaction were studied. In this mechanism there is reversible formation of an inactive form of the second complex along the pathway. This substrate-induced inactivation typically results in the progress curve showing a burst. Three parameters can be obtained from the progress curve: the initial rate, the final rate and the rate constant characterizing the transient. The rate constant for the conversion of the inactive form of the complex into the active form can be obtained either from these parameters or by measuring the regain of enzymic activity. The partition ratio can also be obtained from the three parameters; this is the ratio of the rate of conversion of complex into product to the rate of conversion of complex into inactive form. Simulations give guidance to the conditions required for accurate determinations of the rate constants.

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Year:  1991        PMID: 1930157      PMCID: PMC1151550          DOI: 10.1042/bj2790087

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


  26 in total

1.  On the kinetics of suicide substrates.

Authors:  M A Burke; P K Maini; J D Murray
Journal:  Biophys Chem       Date:  1990-08-31       Impact factor: 2.352

Review 2.  Slow transitions and hysteretic behavior in enzymes.

Authors:  C Frieden
Journal:  Annu Rev Biochem       Date:  1979       Impact factor: 23.643

3.  Kinetic aspects of regulation of metabolic processes. The hysteretic enzyme concept.

Authors:  C Frieden
Journal:  J Biol Chem       Date:  1970-11-10       Impact factor: 5.157

4.  Acquisition of substrate-specific parameters during the catalytic reaction of penicillinase.

Authors:  N Citri; A Samuni; N Zyk
Journal:  Proc Natl Acad Sci U S A       Date:  1976-04       Impact factor: 11.205

5.  Interaction between serine beta-lactamases and class A substrates: a kinetic analysis and a reaction pathway hypothesis.

Authors:  J M Frère
Journal:  Biochem Pharmacol       Date:  1981-03-15       Impact factor: 5.858

6.  Mechanism of substrate-induced inactivation of beta-lactamase I.

Authors:  P A Kiener; V Knott-Hunziker; S Petursson; S G Waley
Journal:  Eur J Biochem       Date:  1980-08

7.  Hysteretic enzymes.

Authors:  K E Neet; G R Ainslie
Journal:  Methods Enzymol       Date:  1980       Impact factor: 1.600

8.  Kinetics of suicide substrates.

Authors:  S G Waley
Journal:  Biochem J       Date:  1980-03-01       Impact factor: 3.857

9.  Kinetic studies on the inactivation of Escherichia coli RTEM beta-lactamase by clavulanic acid.

Authors:  J Fisher; R L Charnas; J R Knowles
Journal:  Biochemistry       Date:  1978-05-30       Impact factor: 3.162

10.  Inhibition of the RTEM beta-lactamase from Escherichia coli. Interaction of enzyme with derivatives of olivanic acid.

Authors:  R L Charnas; J R Knowles
Journal:  Biochemistry       Date:  1981-05-12       Impact factor: 3.162

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  14 in total

1.  Site-directed mutagenesis and substrate-induced inactivation of beta-lactamase I.

Authors:  S J Thornewell; S G Waley
Journal:  Biochem J       Date:  1992-12-15       Impact factor: 3.857

2.  An amino acid position at crossroads of evolution of protein function: antibiotic sensor domain of BlaR1 protein from Staphylococcus aureus versus clasS D β-lactamases.

Authors:  Malika Kumarasiri; Leticia I Llarrull; Oleg Borbulevych; Jennifer Fishovitz; Elena Lastochkin; Brian M Baker; Shahriar Mobashery
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3.  Substrate-induced inactivation of the Escherichia coli AmiD N-acetylmuramoyl-L-alanine amidase highlights a new strategy to inhibit this class of enzyme.

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4.  Major proteinase movement upon stable serpin-proteinase complex formation.

Authors:  E Stratikos; P G Gettins
Journal:  Proc Natl Acad Sci U S A       Date:  1997-01-21       Impact factor: 11.205

5.  Mechanism and kinetics of inducible nitric oxide synthase auto-S-nitrosation and inactivation.

Authors:  Brian C Smith; Nathaniel B Fernhoff; Michael A Marletta
Journal:  Biochemistry       Date:  2012-01-24       Impact factor: 3.162

6.  Substrate-induced inactivation of the OXA2 beta-lactamase.

Authors:  P Ledent; J M Frère
Journal:  Biochem J       Date:  1993-11-01       Impact factor: 3.857

7.  Directed evolution of protein switches and their application to the creation of ligand-binding proteins.

Authors:  Gurkan Guntas; Thomas J Mansell; Jin Ryoun Kim; Marc Ostermeier
Journal:  Proc Natl Acad Sci U S A       Date:  2005-08-01       Impact factor: 11.205

8.  The kinetics of non-stoichiometric bursts of beta-lactam hydrolysis catalysed by class C beta-lactamases.

Authors:  M G Page
Journal:  Biochem J       Date:  1993-10-01       Impact factor: 3.857

9.  Interaction of oxyimino beta-lactams with a class C beta-lactamase and a mutant with a spectrum extended to beta-lactams.

Authors:  M Nukaga; K Tsukamoto; H Yamaguchi; T Sawai
Journal:  Antimicrob Agents Chemother       Date:  1994-06       Impact factor: 5.191

10.  Exposing a β-Lactamase "Twist": the Mechanistic Basis for the High Level of Ceftazidime Resistance in the C69F Variant of the Burkholderia pseudomallei PenI β-Lactamase.

Authors:  Krisztina M Papp-Wallace; Scott A Becka; Magdalena A Taracila; Marisa L Winkler; Julian A Gatta; Drew A Rholl; Herbert P Schweizer; Robert A Bonomo
Journal:  Antimicrob Agents Chemother       Date:  2015-11-23       Impact factor: 5.191

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