By Alton Meister
Advances in Enzymology and similar parts of Molecular Biology is a seminal sequence within the box of biochemistry, delivering researchers entry to authoritative reports of the newest discoveries in all parts of enzymology and molecular biology. those landmark volumes date again to 1941, offering an unequalled view of the historic improvement of enzymology. The sequence bargains researchers the most recent knowing of enzymes, their mechanisms, reactions and evolution, roles in complicated organic procedure, and their program in either the laboratory and undefined. every one quantity within the sequence gains contributions by way of major pioneers and investigators within the box from world wide. All articles are rigorously edited to make sure thoroughness, caliber, and clarity.
With its wide selection of subject matters and lengthy ancient pedigree, Advances in Enzymology and similar components of Molecular Biology can be utilized not just via scholars and researchers in molecular biology, biochemistry, and enzymology, but additionally through any scientist drawn to the invention of an enzyme, its houses, and its applications.
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Additional resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 50
10). On the other hand, it should be noted that actual tautomerization is not essential for operation of the mechanism of equation 10. A partial protonation of the carbonyl group of Thr 216 would induce a partial positive charge on the Gly 217 NH group. The latter could then pair with the carboxylate group of Asp 32 with an overall effect similar to that of tautomerization. In fact, tautomerization and charge pairing are closely related phenomena. V. Aspartate Aminotransferases This important enzyme, which transfers amino groups from aspartic acid to a-ketoglutarate has been studied extensively (27).
The absorption band of the bound pyridoxal phosphate has been established as that of a Schiff base with the c-amino group of lysine 258. At low pH, its peak is at 430 nm and above the pK at 362 nm. The change corresponds to dissociation of a protonated imine nitrogen (9a or 9b --,9c). It is not clear whether the conformation is that of 9a or 9b (38,39). While the conformation could change upon deprotonation, observations of polarized light spectra in crystals of the enzyme (40) suggest that it does not.
One-letter abbreviations have been used for the amino acids. Based on a diagram of Lardner et al. (64). side-chain amide of Asn 44 in the @ sheet through the substrate and into the C-terminus of the long a helix present in the molecule (67). An examination of the structures of proteins containing bound coenzymes or prosthestic groups reveals that in almost every instance there is at least one carbonyl or NH of a peptide group bound to the TAUTOMERISM IN ENZYMATIC CATALYSIS 29 coenzyme. In the dehydrogenases one or more OH groups of the ribose ring of the pyridine nucleotide are bound (68,69).
Advances in Enzymology and Related Areas of Molecular Biology, Volume 50 by Alton Meister