Regulation of proteolytic activity by engineered tridentate metal binding loops

Journal of the American Chemical Society

Volumn 118, Issue 5, 1996, Pages 1227-1228

  Halfon, Sherin ^a   Craik, Charles S ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

SERINE PROTEINASE; TRYPSIN;

AMINO ACID SEQUENCE; ARTICLE; ENZYME ACTIVE SITE; ENZYME STRUCTURE;

EID: 0029916620     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9533813     Document Type: Article

References (10)

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2. (b) Watt, K. W. K.; Lee, P. J.; M'Timkulu, T.; Chan, W. P.; Loor, R. Proc. Natl. Acad. Sci. U.S.A. 1986, 83, 3166.
3. (c) Bhoola, K. D.; Figueroa, C. D.; Worthy, K. Pharmacol. Rev. 1992, 44. 1 and references therein.
4. The relatively weak inhibition of wild-type trypsin by copper(II) may be due to chelation of the metal by the active site residues His-57 and Asp-102. A similar phenomenon is seen with Ag(I), which was demonstrated to bind to these residues by X-ray crystallography. Chambers, J. L.; Cristoph, G. G.; Krieger, M.; Kay, L.; Stroud, R. M. Biochem. Biophys. Res. Commun. 1974, 59, 70.
5. Sprang, S.; Standing, T.; Fletterick, R. J.; Stroud, R. M.; Finer-Moore, J.; Xuong, N-H.; Hamlin, R.; Rutter, W. J.; Craik, C. S. Science 1987, 237, 905.
6. Fujinaga, M.; James, M. N. G. J. Mol. Biol. 1987, 195, 373.
7. Cregg, J. M.; Vedvick, T. S.; Raschke, W. C. Biotechnology 1993, 11, 905.
8. Higaki, J. N.; Haymore, B. L.; Chen, S.; Fletterick, R. J.; Craik, C. S. Biochemistry 1990, 29, 8582.
9. TnTo2 is glycosylated by this expression system. Cleavage of the sugar moiety by N-glycosidase F gave the expected molecular weight (supporting information).
10. Chemical Society (Great Britain). Stability Constants of Metal-Ion Complexes, Supplement I: The Chemical Society: London. 1971; p 281.