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Transition‐state analogues of aminoacyl adenylates

1978; Wiley; Volume: 91; Issue: 2 Linguagem: Inglês

10.1016/0014-5793(78)81184-3

1873-3468

A.I. Biryukov, B.Kh. Ishmuratov, R. M. Khomutov,

Enzyme Structure and Function

FEBS LettersVolume 91, Issue 2 p. 249-252 Full-length articleFree Access Transition-state analogues of aminoacyl adenylates A.I. Biryukov, A.I. Biryukov Institute of Molecular Biology, USSR Academy of Sciences, Moscow 117312, USSRSearch for more papers by this authorB.Kh. Ishmuratov, B.Kh. Ishmuratov Institute of Molecular Biology, USSR Academy of Sciences, Moscow 117312, USSRSearch for more papers by this authorR.M. Khomutov, Corresponding Author R.M. Khomutov Institute of Molecular Biology, USSR Academy of Sciences, Moscow 117312, USSRTo whom reprint requests should be addressedSearch for more papers by this author A.I. Biryukov, A.I. Biryukov Institute of Molecular Biology, USSR Academy of Sciences, Moscow 117312, USSRSearch for more papers by this authorB.Kh. Ishmuratov, B.Kh. Ishmuratov Institute of Molecular Biology, USSR Academy of Sciences, Moscow 117312, USSRSearch for more papers by this authorR.M. Khomutov, Corresponding Author R.M. Khomutov Institute of Molecular Biology, USSR Academy of Sciences, Moscow 117312, USSRTo whom reprint requests should be addressedSearch for more papers by this author First published: July 15, 1978 https://doi.org/10.1016/0014-5793(78)81184-3Citations: 14AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat References 1 D. Cassio, F. Lemoine, J.-P. Waller, E. Sandrin, R. Boissonnas, Biochemistry, 6, (1967), 827– 835. 2 R.M. Khomutov, T.I. Osipova, A.I. Biryukov, B.Kh. Ishmuratov, Bioorg. Khim., (1978), in press 3 M. Yaniv, F. Gros, J. Mol. Biol., 44, (1969), 1– 15. 4 M.P. Stulberg, J. Biol. Chem., 242, (1967), 1060– 1064. 5 P. Lemoine, J.-P. Waller, R. Van Rapenbusch, Eur. J. Biochem., 4, (1968), 213– 221. 6 S. Gutcho, Biochim. Biophys. Acta, 157, (1968), 76– 82. 7 J.C. Gillam, G.M. Tener, Methods Enzymol., 20, (1971), 55– 70. 8 F.H. Bergmann, P. Berg, M. Dieckmann, J. Biol. Chem., 236, (1961), 1735– 1740. 9 A.D. Kelmes, G.D. Nevelli, M.P. Stulberg, J. Biol. Chem., 240, (1965), 3979– 3983. 10 H. Lineweaver, D. Burk, J. Am. Chem. Soc., 56, (1934), 658– 666. 11 M. Tamari, A. Cassaigne, A.-M. Lacoste, E. Neuzil, Biochimie, 57, (1975), 97– 103. 12 T.I. Osipova, A.I. Biryukov, I.A. Gandurina, N.B. Tarusova, R.M. Khomutov, Bioorg. Khim., (1978), in press 13 W.P. Jenks, N.O. Kaplan E.P. Kennedy Current Aspects of Biochemical Energetics (1966), Academic Press 273– 298. 14 R.M. Khomutov, Symp. Structure and Function of Peptides and Proteins, (1967), 69– Riga 15 R.M. Khomutov, 5th Int. Symp. Chemistry of Natural Products, (1968), 210– 211. London 16 R. Wolfenden, Ann. Rev. Biophys. Bioenerg., 5, (1976), 271– 306. 17 N.B. Tarusova, M.K. Kukhanova, R.M. Khomutov, Bioorg. Khim., (1978), in press Citing Literature Volume91, Issue2July 15, 1978Pages 249-252 ReferencesRelatedInformation