Literature DB >> 6625178

Fitting enzyme-kinetic data to V/K.

D B Northrop.   

Abstract

Kinetic data from enzyme-catalyzed reactions have been analyzed traditionally in terms of the Michaelis-Menten equation, which assumes that the maximal velocity (V) and the Michaelis constant (K) are the primary kinetic constants. But what is needed from most kinetic studies today is V/K. A new form of the equation is proposed which assumes that V and V/K are the primary kinetic constants: v = (V . S . V/K)/(V + S . V/K). Computer fittings of both experimental and simulated velocity data to both equations give results favoring the new equation.

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Year:  1983        PMID: 6625178     DOI: 10.1016/0003-2697(83)90034-9

Source DB:  PubMed          Journal:  Anal Biochem        ISSN: 0003-2697            Impact factor:   3.365


  7 in total

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2.  The determination of specificity constants in enzyme-catalysed reactions.

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5.  Temperature-related kinetic differentiation of glucosephosphate isomerase alleloenzymes isolated from the blue mussel, Mytilus edulis.

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7.  1,3-Butadiene: linking metabolism, dosimetry, and mutation induction.

Authors:  J A Bond; G A Csanady; M L Gargas; F P Guengerich; T Leavens; M A Medinsky; L Recio
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  7 in total

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