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 reports of the most recent discoveries in all parts of enzymology and molecular biology. those landmark volumes date again to 1941, delivering an unmatched view of the old improvement of enzymology. The sequence deals researchers the newest realizing 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 gains contributions through best pioneers and investigators within the box from world wide. All articles are rigorously edited to make sure thoroughness, caliber, and clarity.
With its wide variety of themes and lengthy historic pedigree, Advances in Enzymology and comparable components of Molecular Biology can be utilized not just by means of scholars and researchers in molecular biology, biochemistry, and enzymology, but additionally by way 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 50
This type of conformational isomerism has recently been suggested by Jones (79) on the basis of spectroscopic studies of N-alkylmethoxyacetamides. The imidazole group of a histidine residue or an amide group of aspartate could rotate in a similar manner to connect a new hydrogenbonded pathway. Recently it was suggested that the net transport of protons through proteins of membranes may occur by a process involving 31 TAUTOMERISM IN ENZYMATIC CATALYSIS Y Fig. 6. Scheme showing how rotation of a serine or threonine side chain could switch one hydrogen-bonded pathway to another.
METZLER anion is able to accept a proton on either oxygen or nitrogen to give both tautomers l a and l c. At 25°C in aqueous solution the two are present in almost equal amounts (1,2). (la) Q-0 -0 0 H+ H+ As indicated by the two resonance structures of the dipolar ion lc, the electrons of the anionic center are delocalized into the ring. 3 in lc. An important consequence of this difference in pK is that protonation of l c on the oxygen at neutral p H causes release of the proton on the nitrogen, that is, l c is tautomerized to la.
In carboxypeptidase, the Znz+ ion at the active site is surrounded by two imidazole groups of histidine side chains. These in turn are hydrogen bonded in the same fashion as in hemoglobin to amide groups of the protein (73). The same is true of the iron-sulfur proteins. The sulfur atoms of the cysteine side chains not only bond to the iron atoms of the electron-accepting Fe4S4center, but are hydrogen bonded to N H groups of the protein (74,75). The so-called nucleotide-binding domain of dehydrogenases and of a variety of other enzymes is of special interest.