By Alton Meister
Advances in Enzymology and comparable parts of Molecular Biology is a seminal sequence within the box of biochemistry, providing 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, delivering an unmatched view of the historic improvement of enzymology. The sequence bargains researchers the newest figuring out of enzymes, their mechanisms, reactions and evolution, roles in advanced organic approach, and their program in either the laboratory and undefined. each one quantity within the sequence positive aspects contributions via best pioneers and investigators within the box from around the globe. All articles are conscientiously edited to make sure thoroughness, caliber, and clarity.
With its wide selection of issues and lengthy old pedigree, Advances in Enzymology and comparable parts of Molecular Biology can be utilized not just by means of scholars and researchers in molecular biology, biochemistry, and enzymology, but additionally by means of any scientist drawn to the invention of an enzyme, its houses, and its purposes.
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Additional info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 42
It is widely accepted that the biotin moiety of all biotinyl-enzymes is covalently bound to the c-NH, group of a lysine (55). However, it is not clear whether there are further similarities in the biotin-bearing sites of the various biotin-enzymes. For example, there is no evidence at present concerning possible common primary structures of the areas immediately adjacent to the biotin-lysine moiety. T h e finding of relatively small polypeptides carrying biotin in acetyl-CoA carboxylase and transcarboxylase initially suggested that such carrier peptides might be a common feature of biotin-enzymes (1 1 l ) , but even here the apparently native forms of the two polypeptides vary considerably in size [ca.
Wvalues were determined in a solvent similar to the reaction mixture which was used in the reacting enzyme sedimentation studies, except that ADP replaced ATP. Comparison of the values obtained by the two methods shows general agreement in all cases TABLE VII Reacting Form of Different Pyruvate Carboxylasea Data from references 33, 46, 103, and 149. Sedimentation coefficient Species Chicken liver Turkey liver Calf liver Rat liver Yeast P . cilromellolis A . globiformis A . vinelandii Protein, ~ ~ 2 0 .
T h e characteristics of the binding curve for acetyl-CoA and its relationship to the catalytic response to increasing concentrations of acetylCoA is also of importance in elucidating the mechanism of activation. 0 (133). 2 38 M E R T O N F . I T I ' E R . R O L A N D E BARDEN. A N D RARRY L TAYLOR which compares well with the K , of about 13 p M at this pH. Thus, the binding and activation relationships appear to be very similar. T w o points must be noted, however. T h e protein concentration is necessarily several orders of magnitude higher in the binding experiments than in the catalytic measurements, and the binding experiments were carried out thus far in the absence of substrates.