Literature DB >> 5943446

Allosteric enzyme models and their analysis by the theory of graphs.

M V Volkenstein, B N Goldstein.   

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Year:  1966        PMID: 5943446     DOI: 10.1016/0304-4165(66)90446-6

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


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  4 in total

1.  A novel approach to distinguish between enzyme mechanisms: quasi-steady-state kinetic analysis of the prostaglandin H synthase peroxidase reaction.

Authors:  Peter V Vrzheshch; Elena A Batanova; Alevtina T Mevkh; Sergei D Varfolomeev; Irina G Gazaryan; Roger N F Thorneley
Journal:  Biochem J       Date:  2003-06-15       Impact factor: 3.857

2.  Theoretical approach to the steady-state kinetics of a bi-substrate acyl-transfer enzyme reaction that follows a hydrolysable-acyl-enzyme-based mechanism. Application to the study of lysophosphatidylcholine:lysophosphatidylcholine acyltransferase from rabbit lung.

Authors:  J Martín; J Pérez-Gil; C Acebal; R Arche
Journal:  Biochem J       Date:  1990-02-15       Impact factor: 3.857

3.  Conformational transitions in human AP endonuclease 1 and its active site mutant during abasic site repair.

Authors:  Lyubov Yu Kanazhevskaya; Vladimir V Koval; Dmitry O Zharkov; Phyllis R Strauss; Olga S Fedorova
Journal:  Biochemistry       Date:  2010-08-03       Impact factor: 3.162

4.  Generating rate equations for complex enzyme systems by a computer-assisted systematic method.

Authors:  Feng Qi; Ranjan K Dash; Yu Han; Daniel A Beard
Journal:  BMC Bioinformatics       Date:  2009-08-04       Impact factor: 3.169

  4 in total

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