By Alton Meister
Advances in Enzymology and similar components of Molecular Biology is a seminal sequence within the box of biochemistry, delivering researchers entry to authoritative experiences of the newest discoveries in all parts of enzymology and molecular biology. those landmark volumes date again to 1941, offering an unmatched view of the ancient improvement of enzymology. The sequence deals researchers the most recent knowing of enzymes, their mechanisms, reactions and evolution, roles in advanced organic procedure, and their program in either the laboratory and undefined. each one quantity within the sequence good points contributions via 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 subject matters and lengthy ancient pedigree, Advances in Enzymology and similar parts of Molecular Biology can be utilized not just via scholars and researchers in molecular biology, biochemistry, and enzymology, but in addition via any scientist drawn 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 45
Wt. subunit increases correspondingly. 5 mM palmitoyl-CoA, only the inactive subunit remains. T w o protein peaks are seen at intermediate, partially inhibitory palmitoyl-CoA concentrations. T h e lower-molecular-weight peak (subunit) contains radioactive palmitoyl-CoA, but the intact synthetase does not. Apparently, highaffinity binding sites for palmitoyl-CoA become exposed only on dissociation. Dialysis does not remove the bound inhibitor nor does it restore synthetase activity. However, active, high-molecular-weight enzyme can be regenerated by dialyzing the isolated, palmitoyl-CoA-containing subunit either against MMPor (2,6-di-Omethyl)@-cyclodextrin, one of the agents that complexes palmitoyl-CoA in effective competition with protein (57,58) (see also Section VIII).
It should be noted, however, that the agents to be described, unlike polysaccharide, affect chain length only in the post-steady state. 4 . Effect of BSA on Chain Length (50) In experiments lasting for 15 min BSA at 1 mg/ml shifts the product pattern of M. smegnatis synthetase, assayed at 300 pM acetyl-CoA and 20 pM malonyl-CoA, from 25 to over 70% short chains (C,4-Cls)r a change of the same order as that produced by polysaccharide under otherwise identical conditions. While tight binding of palmitoyl-CoA and hence an effect on the long-chain transacylase could account for the BSA effect, it is important to note that such chain shortening is seen only relatively late and not during the steady state, which lasts for approximately 2 min (58a).
Hydrolysis lowers the concentration of product (palmitoyl-CoA) already released. T h e relative rates of transacyiation and elongation therefore shift in favor of the former. T h e hypothesis that accounts satisfactorily for all the chainshortening effects described above for the post-steady state is thai the relative rates of two enzymes, the terminating long-chain transacylase and the chain-lengthening condensing enzyme, determine the product pattern by competing for acyl-enzyme. Agents that decrease the concentration of free o r released palmitoyl-CoA, by whatever mechanism, shift the transacylase equilibrium in favor of palmitoyl-CoA at the expense of elongation.
Advances in Enzymology and Related Areas of Molecular Biology, Volume 45 by Alton Meister
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