Angiotensin II-forming activity in a reconstructed ancestral chymase

Science

Volumn 271, Issue 5248, 1996, Pages 502-505

  Chandrasekharan, Unnikrishnan M ^a   Sanker, Subramaniam ^a   Glynias, Manuel J ^a   Karnik, Sadashiva S ^a   Husain, Ahsan ^a  

^a LERNER RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANGIOTENSIN DERIVATIVE; ANGIOTENSIN I; ANGIOTENSIN II; CHYMASE; SERINE PROTEINASE; SYNTHETIC DNA; ANGIOTENSIN;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; BINDING SITE; CHEMISTRY; ENZYME SPECIFICITY; GENETICS; HUMAN; METABOLISM; MOLECULAR EVOLUTION; MOLECULAR GENETICS; RAT; ENZYME ACTIVITY; ENZYME STRUCTURE; EVOLUTION; PRIORITY JOURNAL; PROTEIN EXPRESSION;

AMINO ACID SEQUENCE; ANGIOTENSIN I; ANGIOTENSIN II; ANGIOTENSINS; ANIMALS; BINDING SITES; CHYMASES; EVOLUTION, MOLECULAR; GENES, SYNTHETIC; HUMANS; MOLECULAR SEQUENCE DATA; RATS; SERINE ENDOPEPTIDASES; SUBSTRATE SPECIFICITY;

ANIMALIA;

EID: 0029671221     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.271.5248.502     Document Type: Article

References (22)

1. C F. Reilly, D. A. Tewksbury, N. M. Schechter, J. Travis, J Biol. Chem 257, 8619 (1982)
2. H Urata, A. Kinoshita, K. S. Misono, F. M. Bumpus, A Husain, ibid 265, 22348 (1990).
3. H. Le Trong, H Neurath, R G Woodbury, Proc. Natl. Acad Sci U.S.A. 84, 364 (1987).
4. G. H. Caughey, F Leidig, N. F Viro, J. A Nadel, J Pharmacol. Exp Ther 244, 133 (1938)
5. S D. Brain and T. J Williams, Nature 335, 73 (1988).
6. R. G. Woodbury et al., ibid 312, 450 (1984)
7. A. Kinoshita, H. Urata, F M. Bumpus, A Husain, J. Biol. Chem 266, 19192 (1991)
8. H Urata et al., J. Clin. Invest. 91, 1269 (1993)
9. B D Hoit et al , ibid. 95, 1519 (1995)
10. T M Jermann, J. G. Opitz, J. Stackhouse, S. A. Benner, Nature 374, 57 (1995)
11. D. M. Hillis, J. J. Bull, M E. White, M. R Badgett, I J. Molineux, Science 255, 589 (1992)
12. H G. Khorana, ibid 203, 614 (1979).
13. M Murakami, S. S Karnik, A. Husain, J. Biol. Chem 270, 2218 (1995) and references therein.
14. E. G Erdos and R. A. Skidgel, Biochem. Soc. Trans 13, 42 (1985).
15. I W Henderson, J. A. Oliver, A McKeever, N. Hazon, in Advances in Animal and Comparative Physiology, G. Pethes and V L. Frenyo, Eds (Pergamon, New York, 1981), pp. 355-363.
16. L M Pastor et al., J Submicrosc Cytol Pathol 20, 25 (1988), R Hakanson et al., Histochemistry 86, 5 (1986).
17. L M Pastor et al., J Submicrosc Cytol Pathol 20, 25 (1988), R Hakanson et al., Histochemistry 86, 5 (1986).
18. Abbreviations for the amino acid residues are as follows: A, Ala, C, Cys, D, Asp; E, Glu; F, Phe, G, Gly, H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn, P, Pro, Q, Gln, R, Arg; S, Ser; T, Thr, V, Val, W, Trp, and Y, Tyr
19. D L Swofford, PAUP: Phylogenetic Analysis Using Parsimony, version 3.0 (Center for Biodiversity, Illinois Natural History Survey, Champaign, IL, 1992).
20. J Felsenstein, Evolution 39, 783 (1985).
21. S. J Remmington, R G Woodbury, R A Reynolds, B. W. Matthews, H Neurath, Biochemistry 27, 8097 (1988)
22. Supported by NIH grants HL44201 and HL33713. We thank W Gilbert for helpful criticism, D. Wilk for excellent technical assistance, and C. Kassuba for editorial assistance