Advances in Enzymology and Related Areas of Molecular by Alton Meister PDF

By Alton Meister

ISBN-10: 0470123036

ISBN-13: 9780470123034

ISBN-10: 0471890111

ISBN-13: 9780471890119

Advances in Enzymology and comparable components of Molecular Biology is a seminal sequence within the box of biochemistry, delivering researchers entry to authoritative stories of the most recent discoveries in all components of enzymology and molecular biology. those landmark volumes date again to 1941, supplying an unmatched view of the historic improvement of enzymology. The sequence bargains researchers the newest figuring out of enzymes, their mechanisms, reactions and evolution, roles in complicated organic method, and their program in either the laboratory and undefined. each one quantity within the sequence gains contributions through major pioneers and investigators within the box from worldwide. All articles are conscientiously edited to make sure thoroughness, caliber, and clarity.

With its wide selection of issues and lengthy ancient pedigree, Advances in Enzymology and comparable components of Molecular Biology can be utilized not just by means of scholars and researchers in molecular biology, biochemistry, and enzymology, but additionally by means of any scientist drawn to the invention of an enzyme, its homes, and its applications.

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Additional resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 57

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The agreement between the experimental values, shown as points in Figure 13, and the theoretical lines expected on the basis of these equilibrium constants is satisfactory. Enalaprilat is more potent than captopril as a converting enzyme inhibitor; both compounds are highly potent. 001 - I 2 I 4 I 6 I 8 1 10 I N H I B I T O R , nM Figure 13. Steady-state, first-order rate constants for converting enzyme-catalyzed hydrolysis of furanacryloyl-phe-gly-gly plotted as a function of inhibitor concentration for enalaprilat and captopril; the curves are theoretical fits to appropriate rate laws employing the dissociation constants derived from these data.

3) undergoes this change 3 pH units below enalaprilat, and that Compound 45 has no basic functionality at this critical site at all. One is driven to the conclusion that the bell-shaped pH dependence of the dissociation constants reflects protolytic equilibria involving two groups on the enzyme surface and that, unexpectedly, the state of protonation of the secondary nitrogen atom of enalaprilat makes little or no difference. This does not, of course, imply that there exists no interaction between this nitrogen atom and the enzyme, only that the strength of this interaction does not depend on the state of protonation of this atom.

It seems highly likely that this interaction is with the carboxylate function, rather than via the secondary nitrogen atom (see below). B. STUDIES WITH ANALOGS OF ENALAPRILAT Efforts to understand the detailed nature of the interaction with angiotensin-converting enzyme were aided by looking at several structurally related inhibitors that differ from the parent compound in carefully chosen ways: deletion of a carboxylate function, deletion of the basic NH moiety, alteration in acid-base properties through introduction of novel substituents.

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Advances in Enzymology and Related Areas of Molecular Biology, Volume 57 by Alton Meister


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