By Nord F F (ed)
Advances in Enzymology and similar components of Molecular Biology is a seminal sequence within the box of biochemistry, supplying 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 most recent knowing of enzymes, their mechanisms, reactions and evolution, roles in advanced organic procedure, and their software in either the laboratory and undefined. each one quantity within the sequence positive factors contributions through 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 variety of subject matters and lengthy ancient pedigree, Advances in Enzymology and comparable components of Molecular Biology can be utilized not just by way 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 purposes.
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Additional info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 32
Introduction It has long been recognized that many biological oxidation-reduction reactions require metal ions, but in most cases the function of the metal ion is not clear. However, as a result of recent research, and the application of principles which have proved very successful in achieving an understanding of numerous organic reactions, new proposals for the mechanisms of a number of such redox reactions can be suggested. It would be impossible in an article of this type to survey the mechanisms of all oxidations catalyzed by metalloenzymes.
7). But it is not until carbanion formation that the YH group can donate its proton to the C4, atom owing to a partial negative charge that has arisen on this atom. Experimental evidence indicates that the imidazole ring of a histidine residue may act as such a Y group (32). The Cq, atom acquires tetrahedral configuration on protonation. I ts bonds with the Cq and N atoms are single. This allows the coenzyme ring to rotate back into the original plane, with concomitant reprotonation of the pyridine nitrogen (Scheme l(8, 9)).
3. On the Interaction of the %Methyl Group of PLP with the Protein I t seems plausible t h a t the coenzyme’s 2-methyl group, known not to be essential in model systems, may take part in coenzyme-protein interaction (hydrophobic bonding). I n order to elucidate this question, the kinetics of association of apo-AAT with some alkyl analogs of PLP arid properties of the resulting holoenzymes were studied (28). Alkyl analogs of PLP As shown in Table I, addition to the apoenzyme of any one of the artificial coenzymes (I-IV) results in appearance of a positive Cotton effect in the absorption band of the respective protein-bound Schiff bases.