Theoretical evaluation of a model of the catalytic triads of serine and cysteine proteases by ab initio molecular orbital calculation

Journal of Theoretical Biology

Volumn 196, Issue 4, 1999, Pages 513-519

  Nishihira, Jun ^a   Tachikawa, Hiroto ^b  

^a HOKKAIDO UNIVERSITY   (Japan)

^b HOKKAIDO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; CYSTEINE; CYSTEINE PROTEINASE; HISTIDINE; PROTON; SERINE; SERINE PROTEINASE;

ARTICLE; ENZYME ACTIVE SITE; ENZYME MECHANISM; MODEL; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTON TRANSPORT; THEORETICAL STUDY;

EID: 0033590684     PISSN: 00225193     EISSN: None     Source Type: Journal    
DOI: 10.1006/jtbi.1998.0851     Document Type: Article

References (18)

1. Bazan, J. F. & Fletterick, R. J. (1988). Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: Structural and functional implications. Proc. Nat. Acad. Sci. U.S.A. 85, 7872-7876.
2. Bazan, J. F. & Fletterick, R. J. (1989). Detection of a trypsin-like serine protease domain in flaviviruses and pestiviruses. Virology 171, 637-639.
3. Blow, D. M., Birktoft, J. J. & Hartely, B. S. (1969). Role of a buried acid group in the mechanism of action of chymotrypsin. Nature 221, 337-340.
4. Dougherty, W. G., Parks, T. D., Cary, S. M., Bazan, J. F. & Fletterick, R. J. (1989). Characterization of the catalytic residues of the tobacco etch virus 49-kDa proteinase. Virology 172, 302-310.
5. Garavito, R. M., Rossman, M. G., Argos, P. & Eventoff, W. (1977). Convergence of active center geometries. Biochemistry 16, 5065-5071.
6. Gorbalenya, A. E., Bonchenko, A. P., Blinov, V. M. & Koonin, E. V. (1989). Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases: A distinct protein superfamily with a common structural fold. FEBS Lett. 243, 103-114.
7. Higaki, J. N., Evnin, L. B. & Craik, C. S. (1989). Introduction of a cytsteine protease active site in trypsin. Biochemistry 28, 9256-9263.
8. Husain, S. S. & Lowe, G. (1968). Evidence for histidine in the active site of papain. Biochem. J. 108, 855-859.
9. McGrath, M. E., Wilke, M. E., Higaki, J. N., Craik, C. S. & Fletterick, R. J. (1989). Crystal structure of two engineered thiol trypsin. Biochemistry 28, 9264-9270.
10. Nakagawa, S., Umeyama, H. & Kudo, T. (1980). The molecular orbital study on the role of hydrogen bonding system in the active site of serine proteases. Chem. Pharm. Bull. 28, 1342-1344.
11. Neet, K. E. & Koshland, Jr, D. E. (1966). The conversion of serine at the active site of subtilisin to cysteine: A "chemical mutation". Proc. Nat. Acad. Sci. U.S.A. 56, 1606-1611.
12. Nishihira, J. & Tachikawa, H. (1997). Theoretical study on the interaction between dopamine and its receptor by ab initio molecular orbital calculation. J. Theor. Biol. 185, 157-163.
13. Polgar, L. & Bender, M. L. (1967). The reactivity of thiol-subtilisin, an enzyme containing a synthetic functional group. Biochemistry 6, 610-620.
14. Pople, J. A. & Segal, G. A. (1966). Approximate self-consistent molecular orbital theory. III. CNDO results for AB2 and AB3 systems. J. Chem. Phys. 44, 3289-3296.
15. Storm, D. R. & Koshland, Jr. D. E. (1970). A source for the special catalytic power of enzymes: Orbital steering. Proc. Nat. Acad. Sci. U.S.A. 66, 445-452.
16. Umeyama, H. & Morokuma, K. (1977). The origin of hydrogen bonding. An energy decomposition study. J. Amer. Chem. Soc. 99, 1316-1332.
17. Umeyama, H. & Nakagawa, S. (1980). The molecular orbital study on the role of hydrogen bonding system in the active site of serine proteases. Chem. Pharm. Bull. 28, 2292-2300.
18. Yokosawa, H., Ojima, S. & Ishii, S. (1977). Thioltrypsin: Chemical transformation of the active-site serine residue of streptomyces griseus trypsin to a cysteine residue. J. Biochem. 82, 869-876.