Literature DB >> 4463962

A kinetic analysis of enzyme systems involving four substrates.

K R Elliott, K F Tipton.   

Abstract

A treatment of kinetic data for enzyme mechanisms involving four substrates is described. The initial-rate equations and product-inhibition patterns for such mechanisms are presented. The treatment is extended to include analysis of enzyme mechanisms involving three substrates in which two molecules of one substrate are used.

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Year:  1974        PMID： 4463962      PMCID： PMC1168185          DOI： 10.1042/bj1410789

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


  21 in total

1.  Glutamic dehydrogenase. III. The order of substrate addition in the enzymatic reaction.

Authors:  C FRIEDEN
Journal:  J Biol Chem       Date:  1959-11       Impact factor: 5.157

2.  Kinetics of three substrate enzyme systems. Treatment of partially random mechanisms using equilibrium assumptions.

Authors:  F B Rudolph; H J Fromm
Journal:  J Theor Biol       Date:  1973-05       Impact factor: 2.691

3.  On calculation of rate and dissociation constants from kinetic constants for the Ordered Bi Bi mechanism of liver alcohol dehydrogenase.

Authors:  B V Plapp
Journal:  Arch Biochem Biophys       Date:  1973-05       Impact factor: 4.013

4.  Dalziel rate behaviour in ternary-complex mechanisms for enzyme reactions involving two substrates.

Authors:  G Pettersson
Journal:  Biochim Biophys Acta       Date:  1972-07-13

5.  Studies on galactosyltransferase. Kinetic investigations with N-acetylglucosamine as the galactosyl group acceptor.

Authors:  J F Morrison; K E Ebner
Journal:  J Biol Chem       Date:  1971-06-25       Impact factor: 5.157

6.  A simple method for derivation of rate equations for enzyme-catalyzed reactions under the rapid equilibrium assumption or combined assumptions of equilibrium and steady state.

Authors:  S Cha
Journal:  J Biol Chem       Date:  1968-02-25       Impact factor: 5.157

7.  The interpretation of kinetic data for enzyme-catalysed reactions involving three substrates.

Authors:  K Dalziel
Journal:  Biochem J       Date:  1969-09       Impact factor: 3.857

8.  Purification and properties of succinyl-CoA synthetase from Jerusalem artichoke mitochondria.

Authors:  J M Palmer; R T Wedding
Journal:  Biochim Biophys Acta       Date:  1966-01-11

9.  Pig liver pyruvate carboxylase. The reaction pathway for the carboxylation of pyruvate.

Authors:  G B Warren; K F Tipton
Journal:  Biochem J       Date:  1974-05       Impact factor: 3.857

10.  Kinetic studies of bovine liver carbamoyl phosphate synthetase.

Authors:  K R Elliott; K F Tipton
Journal:  Biochem J       Date:  1974-09       Impact factor: 3.857
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  4 in total

1.  Kinetic studies of bovine liver carbamoyl phosphate synthetase.

Authors:  K R Elliott; K F Tipton
Journal:  Biochem J       Date:  1974-09       Impact factor: 3.857

2.  Product inhibition studies on bovine liver carbamoyl phosphate synthetase.

Authors:  K R Elliott; K F Tipton
Journal:  Biochem J       Date:  1974-09       Impact factor: 3.857

3.  Purification of porphobilinogen deaminase from Euglena gracilis and studies of its kinetics.

Authors:  D C Williams; G S Morgan; E McDonald; A R Battersby
Journal:  Biochem J       Date:  1981-01-01       Impact factor: 3.857

Review 4.  Parameter Reliability and Understanding Enzyme Function.

Authors:  Andrew G McDonald; Keith F Tipton
Journal:  Molecules       Date:  2022-01-01       Impact factor: 4.411
  4 in total

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