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By Alton Meister

Advances in Enzymology and similar components of Molecular Biology is a seminal sequence within the box of biochemistry, providing researchers entry to authoritative studies of the newest discoveries in all parts of enzymology and molecular biology. those landmark volumes date again to 1941, supplying an unmatched view of the old improvement of enzymology. The sequence bargains researchers the newest knowing of enzymes, their mechanisms, reactions and evolution, roles in advanced organic approach, and their program in either the laboratory and undefined. every one quantity within the sequence gains contributions by means of major pioneers and investigators within the box from all over the world. All articles are conscientiously edited to make sure thoroughness, caliber, and clarity.

With its wide selection of themes and lengthy historic pedigree, Advances in Enzymology and comparable components of Molecular Biology can be utilized not just via scholars and researchers in molecular biology, biochemistry, and enzymology, but additionally via any scientist drawn to the invention of an enzyme, its houses, and its purposes.


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A N D BARRY L. OR Recent recalculations of the water proton relaxation data by Scrutton et al. (62) are also consistent with the view that the pyruvate molecule is considerably more distant from the metal ion than was originally proposed. T h e new calculations employ an experimentally determined value for the correlation time (3 x lo-’ sec) rather than an assumed range of times (10-10-10-’2 sec) as had originally been donc. 3. Accordingly, the hypothesis that pyruvate forms a coordination complex with the metal ion by displacing water molecules from the coordination sphere is no longer tenable.

Most other divalent metal ions act as inhibitors rather than activators. All pyruvate carboxylases examined thus far are activated by a monovalent cation with K + , Rb+, Cs+, and NH,+ serving with varying degrees of effectiveness (44,46,50,64,84,88). T h e monovalent cation has a role in catalysis at the site for the Bi-Bi partial reaction (reaction 2), as indicated by the following observations. First, no exchange of [“CIADP or [=P]phosphate into ATP was detected with the rat liver enzyme when K + was excluded from the assay mixture (65).

R O L A N D E BARDEN. A N D RARRY L TAYLOR which compares well with the K , of about 13 p M at this pH. Thus, the binding and activation relationships appear to be very similar. T w o points must be noted, however. T h e protein concentration is necessarily several orders of magnitude higher in the binding experiments than in the catalytic measurements, and the binding experiments were carried out thus far in the absence of substrates. It is possible that the K , may change in the presence of substrates.

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