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Steady‐state kinetics of enzyme‐catalyzed copolymerization on primers
Author(s) -
Bloomfield V.
Publication year - 1966
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1966.360040608
Subject(s) - copolymer , chemistry , kinetics , monomer , reactivity (psychology) , steady state (chemistry) , polymer chemistry , polynucleotide phosphorylase , thermodynamics , enzyme kinetics , catalysis , enzyme , organic chemistry , polymer , active site , purine nucleoside phosphorylase , medicine , physics , alternative medicine , pathology , quantum mechanics , purine
The theory of the steady‐state kinetics of irreversible enzyme‐catalyzed homopolymerization and copolymerization on primers has been developed. The rate law for homopolymerization is of the Michaelis‐Menten form, but the kinetic parameters depend on primer concentration. Copolymerization has been treated for two monomers considering both terminal and penultimate effects and for four monomers considering terminal effects. The composition equations and conditional probabilities for monomer succession are identical for enzymatic and nonenzymatic processes, because the steady‐state approximation is used in both cases. The reactivity ratios and steady‐state velocities are different, however. Examination of published results for AU and UG copolymers synthesized by polynucleotide phosphorylase permits evaluation of reactivity ratios for the AU copolymer and indicates that penultimate effects may be operative in both cases.