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 stories of the most recent discoveries in all parts of enzymology and molecular biology. those landmark volumes date again to 1941, supplying an unequalled view of the ancient improvement of enzymology. The sequence bargains researchers the most recent realizing 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 gains contributions by means of 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 subject matters and lengthy old 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 in addition by means of any scientist drawn to the invention of an enzyme, its houses, and its applications.
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Extra info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 54
Reprinted with permission from reference 52). approach was adopted (44). A number of proteins were examined as substrates for amine incorporation by factor XIIIa. Of those tested, bovine 0-casein proved to be the most effective. The position in &casein of the glutamine residue most susceptible to the action of factor XIIIa was determined and several enzymic and synthetic fragments of 0-casein that contain this glutamine residue were prepared. Of these peptide fragments, each of which proved to be an effective substrate for factor XIIIa, the synthetic pentadecapeptide Ser-Val-Leu-Ser-Leu-Ser-Gln-SerLys-Val-Leu-Pro-ValPro-Glu was the most effective.
Comparison of specificities for fl-acetyl heptapeptides that can assume similar spatial orientations for the side chains and a-hydrogen atoms of lysine and leucine residues upon arrangement of their polypeptide chains in opposite directions. A replot of certain data of Figure 8. ( A ) Liver transglutaminase. (B) Factor XIIIa. The forms of the optically active amino acid residues are given above the bars and refer, respectively, to the residues in the sequence shown. specificity, albeit without loss in stereospecificity, is evident from comparison of the constants for e-aminocaproic acid and its methyl ester and those for the a-hydroxy-E-aminocaproic acids and their methyl esters.
Based on this binding concept, the most reasonable arrangement for D-glutamine residues has the Aa and Ga sites occupied with the proper groups, the a-hydrogen in the carboxamide side chain site, and the carboxamide side chain projecting away from the enzyme molecule. An alternative mode, albeit a seemingly less likely one, would place the a-acylamido €-(7-GLUTAMYL) LYSINE BOND FORMATION 25 and carboxamide groups in their proper sites, leaving the a-hydrogen at Ga and the a-glutaminylamido group pointing away from the molecule.
Advances in Enzymology and Related Areas of Molecular Biology, Volume 54 by Alton Meister