By Alton Meister
Advances in Enzymology and comparable components of Molecular Biology is a seminal sequence within the box of biochemistry, delivering researchers entry to authoritative studies of the most recent discoveries in all components of enzymology and molecular biology. those landmark volumes date again to 1941, delivering an unequalled view of the ancient improvement of enzymology. The sequence deals researchers the newest figuring out of enzymes, their mechanisms, reactions and evolution, roles in complicated organic strategy, and their software in either the laboratory and undefined. every one quantity within the sequence beneficial properties contributions by means of top pioneers and investigators within the box from world wide. All articles are conscientiously edited to make sure thoroughness, caliber, and clarity.
With its wide selection of themes and lengthy ancient pedigree, Advances in Enzymology and comparable parts of Molecular Biology can be utilized not just by way of scholars and researchers in molecular biology, biochemistry, and enzymology, but in addition by means of any scientist attracted to the invention of an enzyme, its homes, and its applications.
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Extra resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 54
13). The net effect would be a specificity lower than that for those D-lysine peptides that are able to associate in two productive modes. It is obvious from examination of the data of Figure 8 that pronounced differences in specificity occur upon replacement by a D-leucine residue of the L-leucine residue on the amino side of, and directly adjacent to, E-(-/-GLUTAMYL) LYSINE BOND FORMATION 49 the substrate lysine residue. The effect is a lowering of specificity for L-lysine, as well as a loss in stereopreference for the L-isomer.
The similarities in specificities toward these compounds, the structures of which vary considerably, would seem to rule out strong binding as being responsible for the observed stereospecificity toward lysine residues. Rather, one would be inclined to conclude that the preference for Llysine residues occurs as a consequence of an unobstructed fit on the enzyme intermediate surface of groups attached to the a-carbon atom of L-lysine. Parenthetically, the lower specificity for D-lysine residues would derive from obstacles on the surface to the most productive arrangement of groups attached to the asymmetric carbon atom of D-lysine.
The data for the straight-chain amines and for their w-methyl branched-chain homologs are plotted together and as functions of increasing amine chain length. The pattern of amine specificity for each enzyme intermediate is the same. Each shows little variation in specificity with chain length for the straight-chain amines and a progressive increase in specificity with increasing chain length for the isobranched-chain amines. The short straight-chain aliphatic amines are much better substrates for each of the enzyme intermediates than are their branched-chain homologs.
Advances in Enzymology and Related Areas of Molecular Biology, Volume 54 by Alton Meister