Distance between the basic group of the amino acid residue's side chain in position P1 of trypsin inhibitor CMTI-III and Asp189 in the substrate pocket of trypsin has an essential influence on the inhibitory activity

Biochemical and Biophysical Research Communications

Volumn 240, Issue 3, 1997, Pages 869-871

  Jaśkiewicz, Anna ^a   Lesner, Adam ^a   Rózycki, Jan ^a   Rodziewicz, Sylwia ^a   Rolka, Krzysztof ^a   Ragnarsson, Ulf ^b   Kupryszewski, Gotfryd ^a  

^a UNIVERSITY OF GDA SK   (Poland)

^b UPPSALA UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ASPARTIC ACID; LYSINE; TRYPSIN; TRYPSIN INHIBITOR;

AMINO ACID SEQUENCE; ARTICLE; ENZYME INHIBITION; ENZYME SUBSTRATE; PRIORITY JOURNAL;

EID: 0031587414     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.1997.7752     Document Type: Article

References (9)

1. Polanowski A. Acta Biochim. Pol. 27:1980;371-382.
2. Wilusz T. Hoppe-Seyler's Z. Physiol. Chem. 364:1983;93-95.
3. Rolka K. Biol. Chem. Hoppe-Seyler. 370:1989;499-502.
4. Rolka K. Biol. Chem. Hoppe-Seyler. 373:1992;1055-1060.
5. Empie M. W., Laskowski M. Jr. Biochemistry. 21:1982;2274-2284.
6. Park S.-J. Effect of Amino Acid Replacement in Ovomucoid Third Domains upon Their Association with Serine Proteinases. 1985;Pardue University, West Lafayette.
7. Otlewski J. Biol. Chem. Hoppe Seyler. 371:1990;589-594.
8. Bode W. FEBS Lett. 242:1988;285-292.
9. Bernstein F. C. J. Mol. Biol. 112:1977;535-542.