New PDF release: Advances in Enzymology and Related Areas of Molecular
By Alton Meister
Advances in Enzymology and comparable components of Molecular Biology is a seminal sequence within the box of biochemistry, providing researchers entry to authoritative stories of the newest discoveries in all components of enzymology and molecular biology. those landmark volumes date again to 1941, delivering an unmatched view of the historic improvement of enzymology. The sequence deals researchers the most recent figuring out of enzymes, their mechanisms, reactions and evolution, roles in complicated organic strategy, and their program in either the laboratory and undefined. each one quantity within the sequence positive aspects contributions via prime 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 historic pedigree, Advances in Enzymology and comparable components of Molecular Biology can be utilized not just through 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 functions.
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Additional resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 44
And Fruton, J. , Biochemistry, 8, 575 (1969). 22. Sachdev, G. , anf Fruton, J. , Biochemistry, 8, 4231 (1969). 23. Sachdev, G. , and Fruton, J. , Biochemistry, 9, 4465 (1970). 24. Ferguson, J. , Andrews, J. , Voynick, I. , and Fruton, J. , I. Biol. , 248, 6701 (1973). 25. Voynick, 1. , and Fruton, J. , Proc. Natl. Acad. Sci. U S . , 68, 257 (1971). 26. Sampath-Kumar, P. , and Fruton, J. , Proc. Natl. Acad. Sci. U S . , 71, 1070 (1974). 27. Raymond, M . , Biochzmie, 54, 145 (1972). 34 ,JOSEPH S FRCTON 28.
Hollands, T. , and Fruton, J. , Bzochemist~y,7, 2045 (1968). 52. Dopheide, T. A. A,, and Jones, W . M . , j . B i d . , 243, 3906 (1968). 53. Page, M . I . , and Jencks, W. , Proc. Natl. Acad. Sci. l J S . , 68, 1678 (1971). 54. Jencks, W. , and Page, M. I . , in Enzymes: Structure and Functzon, J. Drenth, R. A. Osterbaan, and C. , North-Holland, Amsterdam, 1972, p. 45. 55. DaNorn, A,, and Koshland, I). , Biochem. Biophys. Res. Commun. 52, 779 (1973). 56. Fersht, A. , Proc. R o y . Soc. , 8187, 397 (1974).
It is known that pepsin cleaves Z-His-Phe(4N02)-Pla-OMe more rapidly than 2-His-Phe(4N0,)-Phe-OMe (1 07), perhaps because the hydroxylic product is a better leaving group than the amine product. Other explanations for the enhanced reactivity of the Phe(4NOZ)-Pla bond can be offered, but, regrettably, little work has been done on the kinetics of pepsin action on ester substrates. By the same token, if a covalent amino-enzyme intermediate is involved in pepsin catalysis, the acyl portion of the pseudosubstrate should be a good leaving group, and the amino component should be an “unnatural” one.
Advances in Enzymology and Related Areas of Molecular Biology, Volume 44 by Alton Meister