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Altering the specificity of subtilisin B. lentus by combining site-directed mutagenesis and chemical modification
University of Toronto, Canada.ORCID-id: 0000-0002-9577-832X
Vise andre og tillknytning
1996 (engelsk)Inngår i: Bioorganic and Medicinal Chemistry Letters, ISSN 0960-894X, Vol. 6, nr 21, s. 2507-2512Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

The thiol side chain of the M222C mutant of the subtilisin from Bacillus lentus (SBL) has been chemically modified by methyl-, aminoethyl-, and sulfonatoethylthiosulfonate reagents. Introduction of charged residues into the active site of the enzyme reduced the catalytic efficiency with Suc-AAPF-pNA as the substrate, but resulted in better binding of sterically demanding boronic acid inhibitors.

sted, utgiver, år, opplag, sider
1996. Vol. 6, nr 21, s. 2507-2512
Emneord [en]
boronic acid derivative, subtilisin, article, Eggerthella lenta, enzyme activity, enzyme modification, site directed mutagenesis, Bacillus lentus
HSV kategori
Identifikatorer
URN: urn:nbn:se:kth:diva-74867DOI: 10.1016/0960-894X(96)00467-2Scopus ID: 2-s2.0-0030571292OAI: oai:DiVA.org:kth-74867DiVA, id: diva2:490126
Merknad

References: Cornish, V.W., Mendel, D., Schultz, P.G., (1995) Angew. Chem., Int. Ed. Engl., 34, p. 621; Polgar, L., Bender, M.L., (1966) J. Am. Chem. Soc., 88, p. 3153; Neet, K.E., Koshland D.E., Jr., (1966) Proc. Natl. Acad. Sci. USA, 56, p. 1606; Hilvert, D., Kaiser, E.T., (1985) J. Am. Chem. Soc., 107, p. 5805; Radziejewski, C., Ballou, D.P., Kaiser, E.T., (1985) J. Am. Chem. Soc., 107, p. 3352; Stewart, K.D., Radziejewski, C., Kaiser, E.T., (1986) J. Am. Chem. Soc., 108, p. 3480; Rokita, S.E., Kaiser, E.T., (1986) J. Am. Chem. Soc., 108, p. 4984; Kokubo, T., Sassa, S., Kaiser, E.T., (1987) J. Am. Chem. Soc., 109, p. 606; Kaiser, E.T., (1988) Angew. Chem., Int. Ed. Engl., 27, p. 913; Hilvert, D., Hatanaka, Y., Kaiser, E.T., (1988) J. Am. Chem. Soc., 110, p. 682; Wu, Z.-P., Hilvert, D., (1989) J. Am. Chem. Soc., 111, p. 4514; Bell, I.M., Fisher, M.L., Wu, Z.-P., Hilvert, D., (1993) Biochemistry, 32, p. 3754; Peterson, E.B., Hilvert, D., (1995) Biochemistry, 34, p. 6616; Suckling, C.J., Zhu, L.-M., (1993) Bioorg. Med. Chem. Lett., 3, p. 531; Smith, D.J., Kenyon, G.L., (1974) J. Biol. Chem., 249, p. 3317; Kenyon, G.L., Bruice, T.W., (1977) Methods Enzymol., 47, p. 407; Brocklehurst, K., (1979) Int. J. Biochem, 10, p. 259; Bruice, T.W., Kenyon, G.L., (1982) J. Protein Chem., 1, p. 47; Wynn, R., Richards, F.M., (1995) Methods Enzymol., 257, p. 351; Bech, L.M., Breddam, K., (1988) Carlsberg Res. Commun., 53, p. 381; Wynn, R., Harkins, P.C., Richards, F.M., Fox, R.O., (1996) Protein Sci., 5, p. 1026; GrÞn, H., Bech, L.M., Branner, S., Breddam, K., (1990) Eur. J. Biochemistry, 194, p. 897; noteStabile, M.R., Lai, W.G., DeSantis, G., Gold, M., Jones, J.B., Mitchinson, C., Bott, R.R., Liu, C.-C., (1996) Bioorg. Med. Chem. Lett., , in press; noteCleland, W.W., (1964) Biochemistry, 3, p. 480; Graycar, T.P., Bott, R.R., Caldwell, R.M., Dauberman, J.L., Lad, P.J., Power, S.D., Sagar, I.H., Estell, D.A., (1992) Ann. N. Y. Acad. Sci., 672, p. 71; Hsia, C.Y., Ganshaw, G., Paech, C., Murray, C.J., (1996) Anal. Biochem., , in press; Waley, S.G., (1982) Biochem. J., 205, p. 631 NR 20140805

Tilgjengelig fra: 2012-02-03 Laget: 2012-02-03 Sist oppdatert: 2020-01-24bibliografisk kontrollert

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