Appendix: Analysis of pH-dependent kinetics in up to four reactive hydronic states.
作者信息
Brocklehurst S M, Brocklehurst K
机构信息
Department of Chemistry, University of York, Heslington, York, U.K.
出版信息
Biochem J. 1988 Dec 1;256(2):556-8. doi: 10.1042/bj2560556.
Abstract
摘要
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Appendix: Analysis of pH-dependent kinetics in up to four reactive hydronic states.
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引用本文的文献
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Catalytic-site characteristics of the porcine calpain II 80 kDa/18 kDa heterodimer revealed by selective reaction of its essential thiol group with two-hydronic-state time-dependent inhibitors: evidence for a catalytic site Cys/His interactive system and an ionizing modulatory group.
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Structure of chymopapain M the late-eluted chymopapain deduced by comparative modelling techniques and active-centre characteristics determined by pH-dependent kinetics of catalysis and reactions with time-dependent inhibitors: the Cys-25/His-159 ion-pair is insufficient for catalytic competence in both chymopapain M and papain.
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Supracrystallographic resolution of interactions contributing to enzyme catalysis by use of natural structural variants and reactivity-probe kinetics.
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