scholarly journals Computer program for the kinetic equations of enzyme reactions. The case in which more than one enzyme species is present at the onset of the reaction

1991 ◽  
Vol 278 (1) ◽  
pp. 91-97 ◽  
Author(s):  
R Varón ◽  
B H Havsteen ◽  
M García ◽  
F García-Canóvas ◽  
J Tudela

This paper presents an extension of the program developed by Varón, Havsteen, García, García-Cánovas & Tudela [(1990) Biochem. J. 270, 825-828] for the expression of the transient-phase and steady-state kinetic equations of a general enzyme system in which the only enzyme species present at the onset of the reaction is the free enzyme. The program has been extended to situations in which more than one enzyme species may be present at the onset of the reaction. The program is given in Supplementary Publication SUP50165 (5 pages), which has been deposited at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1991) 273, 5.

1985 ◽  
Vol 231 (2) ◽  
pp. 383-387 ◽  
Author(s):  
S C Koerber ◽  
D J Hopper ◽  
W S McIntire ◽  
T P Singer

p-Cresol methylhydroxylases from four different pseudomonads differ in their isoelectric points and, to a lesser extent, in Mr values and substrate specificity. The enzymes from three species were isolated in homogeneous form, then resolved into their flavoprotein and cytochrome subunits, and the subunits were recombined to yield the nine possible hybrids (i.e. three intraspecies and six interspecies). The resulting flavocytochromes showed extensive similarities in steady-state kinetic parameters and in the dissociation constants of their subunits. Evidence is also presented that a fourth type of p-cresol methylhydroxylase, from Pseudomonas putida (N.C.I.B. 9869, form ‘B’), the subunits of which cannot be isolated by the isoelectric focusing technique used to separate the subunits of the other flavocytochromes, nevertheless dissociates slowly at high dilution. The dissociation is reflected by a decline of catalytic activity with time. This process for the ‘B’ enzyme is prevented by the presence of substrate or an excess of a cytochrome subunit isolated from another enzyme species. Incubation of the dissociated subunits with p-cresol brings about extensive, albeit incomplete, re-association and regeneration of activity.


1990 ◽  
Vol 270 (3) ◽  
pp. 825-828 ◽  
Author(s):  
R Varón ◽  
B H Havsteen ◽  
M García ◽  
F García Cánovas ◽  
J Tudela

A versatile computer program with an easy input method has been developed for the construction of the terms in kinetic equations of enzyme reactions. It allows the expression of the time-dependence of the concentrations of all of the species involved as functions of the kinetic parameters. The mathematical theory used in this paper, the program and examples of its use have been deposited as Supplementary Publication SUP 50159 (41 pages) at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1990) 265, 5.


1975 ◽  
Vol 149 (2) ◽  
pp. 313-328 ◽  
Author(s):  
W G Bardsley ◽  
R E Childs

1. The theory of plane curves was applied to the graphical methods used in enzyme kinetics and a mathematical analysis of the possible graph shapes is given. 2. The belief that allosterism can be inferred from steady-state data alone is subjected to criticism and the mathematical significance of sigmoid curves and non-linear double-reciprocal plots is explored. 3. It is suggested that the usual methods of interpreting steady-state kinetic data are often based on over-restrictive assumptions which prevent maximum utilization of the available data. 4. Methods for obtaining the degree of the rate equation from graph shapes obtained directly from initial-rate measurements and from replots of asymptotic behaviour as x → 0 and x → ∞ are discussed. 5. Detailed proofs of the theorems given in the text have been deposited as Supplementary Publication SUP 50049 (10 pages) at the British Library (Lending Division), Boston Spa, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1975), 145, 5.


2007 ◽  
Vol 79 (17) ◽  
pp. 6592-6598 ◽  
Author(s):  
Timothy C. Logan ◽  
Douglas S. Clark ◽  
Timothy B. Stachowiak ◽  
Frantisek Svec ◽  
Jean M. J. Fréchet

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