Tyrosine-83 of human renin contributes to biphasic ph dependence of the renin-angiotensinogen reaction

Bioscience, Biotechnology and Biochemistry

Volumn 63, Issue 6, 1999, Pages 1143-1145

  Nasir, Uddin Mohammad ^a   Suzuki, Fumiaki ^a   Nagai, Takao ^a   Nakagawa, Tsutomu ^a   Nakamura, Yukio ^a  

^a GIFU UNIVERSITY   (Japan)

Author keywords

Catalytic mechanism; Ph dependence; Renin; Tyrosine 83

Indexed keywords

ANGIOTENSINOGEN; RENIN; SERINE PROTEINASE INHIBITOR; TYROSINE;

ANIMAL; ARTICLE; CATALYSIS; CHEMISTRY; HUMAN; KINETICS; PH; SHEEP;

ANGIOTENSINOGEN; ANIMALS; CATALYSIS; HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; RENIN; SERINE PROTEINASE INHIBITORS; SHEEP; TYROSINE;

EID: 0033141673     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.63.1143     Document Type: Article

References (23)

1. Peach, M. J., Renin-angiotensin system: biochemistry and mechanisms of action. Physiol. Rev., 57, 313-370 (1977).
2. Inagami, T., Purification of renin and prorenin. Hypertension, 18, 241-251 (1991).
3. McKown, M. M., Workman, R. J., and Gregerman, R. I., Pep-statin inhibition of human renin. Kinetic studies and estimation of enzyme purity. J. Biol. Chem., 249, 7770-7774 (1974).
4. Misono, K. S. And Inagami, T., Characterization of the active site of mouse submaxillary gland renin. Biochemistry, 19, 2612-2622 (1980).
5. Sielecki, A. R., Hayakawa, K., Fujinaga, M., Murphy, M. E. P., Fraser, M., Muir, A. K., Carilli, C. T., Lewicki, J. A., Baxter, J. D., and James, M. N. G., Structure of recombinant human renin, a target for cardiovascular-active drugs, at 2.5 A resolution. Science, 243, 1346-1351 (1989).
6. Dhanaraj, V., Dealwis, C. G., Frazao, C., Badasso, M., Sibanda, B. L., Tickle, I.J., Cooper, J. B., Driessen, H. P. C., Newman, M., Aguilar, C., Wood, S. P., Blundell, T. L., Hobart, P. M., Geoghegan, K. F., Ammirati, M. J., Danley, D. E., O’Connor, B. A., and Hoover, D. J., X-ray analyses of pep-tide-inhibitor complexes define the structural basis of specificity for human and mouse renins. Nature, 357, 466-472 (1992).
7. Blundell, T. L., Cooper, J. B., Foundling, S. I., Jones, D. M., Atrash, B., and Szelke, M., On the rational design of renin inhibitors: X-ray studies of aspartic proteinases complexed with transition-state analogues. Biochemistry, 26, 5585-5590 (1987).
8. Veerapandian, B., Cooper, J. B., Sali, A., Blundell, T. L., Rosati, R., Dominy, B. W., Damon, D. B., and Hoover, D. J., Direct observation by X-ray analysis of the tetrahedral “intermediate” of aspartic poteinases. Protein Sci., 1, 322-328 (1992).
9. Akawa, J. I., Hiramatsu, R., Nishiyama, M., Horinouchi, S., and Beppu, T., A yeast expression system and site-directed mutagenesis of a fungal aspartic proteinase, Mucor rennin. In “Structure and Function of Aspartic Proteinases”, eds. Dunn, M. B., Plenum Press, New York, pp. 233-242 (1991).
10. Suzuki, F., Goto, K., Shiratori, Y., Inagami, T., Murakami, K., and Nakamura, Y., Tyrosin-83 of renin has an important role in renin-angiotensinogen reaction. Protein Peptide Lett., 3, 45-49 (1996).
11. Nasir, U. M., Takahashi, K., Nagai, T., Nakagawa, T., Suzuki, F., and Nakamura, Y., Two peaks in pH dependence of renin-an-giotensinogen reaction. Biosci. Biotechnol. Bio chem., 62, 338- 340 (1998).
12. Tada, M., Fukamizu, A., Seo, M. S., Takahashi, S., and Murakami, K., Nucleotide sequence of rat renin cDNA. Nucl. Acids. Res., 16, 3576 (1988).
13. Poorman, R. A., Palermo, D. P., Post, L. E., Murakami, K., Kinner, J. H., Smith, C. W., Reardon, I., and Heinrikson, R., Isolation and characterization of native human renin derived from Chinese hamster ovary cells. Proteins: Struct. Fund. Genet., 1, 139-145 (1986).
14. Yamauchi, T., Suzuki, F., Takahashi, A., Tsutsumi, I., Hori, H., Watanabe, T., Ishizuka, Y., Nakamura, Y., and Murakami, K., Expression of rat renin in mammalian cells and its purification. Clin. Exp. Hyper., A14, 377-392 (1992).
15. Nagase, M., Suzuki, F., Fukamizu, A., Takeda, N., Takeuchi, K., Murakami, K., and Nakamura, Y., Sequencing and expression of sheep angiotensinogen cDNA. Biosci. Biotechnol. Biochem., 58, 1884-1885 (1994).
16. Nagase, M., Suzuki, F., Takahashi, A., Fujimori, M., Sawai, Y., and Nakamura, Y., pH-dependent inactivation and reactivation of recombinant sheep angiotensinogen. Biosci. Biotechnol. Biochem., 59, 765-766 (1995).
17. Murakami, K., Suzuki, F., Morita, N., Ito, H., Okamoto, K., Hirose, S., and Inagami, T., High molecular weight renin in stroke-prone spontaneously hypertensive rats Biochim. Biophys. Acta, 622, 115-120 (1980).
18. Suzuki, F., Yamashita, S., Takahashi, A., Ito, M., Miyazaki, S., Nagata, Y., and Nakamura, Y., Highly sensitive microplate-ELISA for angiotensin I using 3,3', 5,5' -tetramethylbenzidine. Clin. Exp. Hyper., All, 83-95 (1990).
19. Suzuki, J., Sasaki, K., Sasao, Y., Hamu, A., Kawasaki, H., Nishiyama, M., Horinouchi, S., and Beppu, T., Alteration of catalytic properties of chymosin by site-directed mutagenesis. Protein Engineering, 2, 563-569 (1989).
20. 75 on the catalytic properties of porcine pepsin A. Protein Peptide Lett., 5, 19-26 (1998).
21. Groves, M. R., Dhanaraj V., Badasso, M., Nugent, P., Pitts, J. E., Hoover D. J., and Blundell, T., A 2.3 A resolution structure of chymosin complexed with a reduced bond inhibitor shows that the active site /Miairpin flap is rearranged when compared with the native crystal structure. Protein Engineering, 11, 833- 840 (1998).
22. James, M. N. G. And Sielecki, A. R., Stereochemical analysis of peptide bond hydrolysis catalyzed by the crystal structure of penicillopepsin. Biochemistry, 24, 3701-3713 (1985).
23. Rauhuel, J., Priestle, J. P., and Gruetter, M. G., The crystal structure of recombinant glycosylated human renin alone and in complex with a transition state analog inhibitor. J. Struct. Biol., 107, 227-236 (1991).