Literature DB >> 6748701

Enzyme specificity: its meaning in the general case.

A Cornish-Bowden.   

Abstract

If an enzyme catalyses two competing reactions, their relative rates are determined by the concentrations of the competing substrates and the two specificity constants, i.e. the catalytic constants for the two substrates divided by the corresponding Michaelis constants. The concept of a specificity constant can be extended to reactions that require two or more substrates: in such cases the specificity for any competing substrate is determined by the apparent specificity constant measured at whatever concentrations of co-substrates, inhibitors, etc., exist under the conditions of competition. The partitioning between two competing substrates is independent of the concentration of any species, such as co-substrate, inhibitor, etc., that reacts only in the part of the mechanism that is common between the competing substrates.

Mesh:

Substances:

Year:  1984        PMID: 6748701     DOI: 10.1016/s0022-5193(84)80045-4

Source DB:  PubMed          Journal:  J Theor Biol        ISSN: 0022-5193            Impact factor:   2.691


  15 in total

1.  Surface potentials and the calculated selectivity of ion channels.

Authors:  Henk Miedema
Journal:  Biophys J       Date:  2002-01       Impact factor: 4.033

2.  Nucleosome competition reveals processive acetylation by the SAGA HAT module.

Authors:  Alison E Ringel; Anne M Cieniewicz; Sean D Taverna; Cynthia Wolberger
Journal:  Proc Natl Acad Sci U S A       Date:  2015-09-23       Impact factor: 11.205

3.  Phylogenetic sequence analysis and functional studies reveal compensatory amino acid substitutions in loop 2 of human ribonucleotide reductase.

Authors:  Andrew J Knappenberger; Sneha Grandhi; Reena Sheth; Md Faiz Ahmad; Rajesh Viswanathan; Michael E Harris
Journal:  J Biol Chem       Date:  2017-08-14       Impact factor: 5.157

4.  Enzyme specificity in reactions of more than one co-substrate.

Authors:  A Cornish-Bowden
Journal:  Biochem J       Date:  1993-04-01       Impact factor: 3.857

5.  Tryptophan Synthase Uses an Atypical Mechanism To Achieve Substrate Specificity.

Authors:  Andrew R Buller; Paul van Roye; Javier Murciano-Calles; Frances H Arnold
Journal:  Biochemistry       Date:  2016-12-13       Impact factor: 3.162

6.  The Basis for Acyl Specificity in the Tafazzin Reaction.

Authors:  Michael Schlame; Yang Xu; Mindong Ren
Journal:  J Biol Chem       Date:  2017-02-15       Impact factor: 5.157

Review 7.  Specificity and nonspecificity in RNA-protein interactions.

Authors:  Eckhard Jankowsky; Michael E Harris
Journal:  Nat Rev Mol Cell Biol       Date:  2015-08-19       Impact factor: 94.444

8.  Metal ion selectivity and substrate inhibition in the metal ion chelation catalyzed by human ferrochelatase.

Authors:  Ruth E Davidson; Christopher J Chesters; James D Reid
Journal:  J Biol Chem       Date:  2009-09-19       Impact factor: 5.157

9.  Optimization of high-throughput sequencing kinetics for determining enzymatic rate constants of thousands of RNA substrates.

Authors:  Courtney N Niland; Eckhard Jankowsky; Michael E Harris
Journal:  Anal Biochem       Date:  2016-06-11       Impact factor: 3.365

10.  Alternative substrate kinetics of Escherichia coli ribonuclease P: determination of relative rate constants by internal competition.

Authors:  Lindsay E Yandek; Hsuan-Chun Lin; Michael E Harris
Journal:  J Biol Chem       Date:  2013-01-28       Impact factor: 5.157

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.