[1] Peptide thioester substrates for serine peptidases and metalloendopeptidases

作者: James C. Powers , Chih-Min Kam

DOI: 10.1016/0076-6879(95)48003-X

关键词:

摘要: Abstract Peptide thioesters are sensitive substrates of various serine peptidases and metalloendopeptidases. Thioester generally have high enzymatic hydrolysis rates low background rates, the can be easily monitored in presence thiol reagents such as 4,4′-dithiodipyridine or 5,5′-dithiobis (2-nitrobenzoic acid). thioester been invaluable for study enzyme specificity inhibitors, especially cases where no other practical synthetic available. Tripeptide type Boc-Ala-Ala-AA-SBzl, AA is nearly all 20 common amino acids, now synthesized should useful subsite mapping new crude cell preparations containing peptidases.

参考文章(38)
J C Powers, B J McRae, T Tanaka, K Cho, R R Cook, Peptide thioesters and 4-nitroanilides as substrates for porcine pancreatic kallikrein Biochemical Journal. ,vol. 220, pp. 569- 573 ,(1984) , 10.1042/BJ2200569
Lin Yu, Edward A. Dennis, Thio-based phospholipase assay. Methods in Enzymology. ,vol. 197, pp. 65- 75 ,(1991) , 10.1016/0076-6879(91)97133-J
T Tanaka, B J McRae, K Cho, R Cook, J E Fraki, D A Johnson, J C Powers, Mammalian tissue trypsin-like enzymes. Comparative reactivities of human skin tryptase, human lung tryptase, and bovine trypsin with peptide 4-nitroanilide and thioester substrates. Journal of Biological Chemistry. ,vol. 258, pp. 13552- 13557 ,(1983) , 10.1016/S0021-9258(17)43949-4
M.J. Smyth, T Wiltrout, J.A. Trapani, K.S. Ottaway, R Sowder, L.E. Henderson, C.M. Kam, J.C. Powers, H.A. Young, T.J. Sayers, Purification and cloning of a novel serine protease, RNK-Met-1, from the granules of a rat natural killer cell leukemia. Journal of Biological Chemistry. ,vol. 267, pp. 24418- 24425 ,(1992) , 10.1016/S0021-9258(18)35783-1
C.M. Kam, B.J. McRae, J.W. Harper, M.A. Niemann, J.E. Volanakis, J.C. Powers, Human complement proteins D, C2, and B. Active site mapping with peptide thioester substrates. Journal of Biological Chemistry. ,vol. 262, pp. 3444- 3451 ,(1987) , 10.1016/S0021-9258(18)61371-7
B.J. McRae, T.Y. Lin, J.C. Powers, Mapping the substrate binding site of human C1r and C1s with peptide thioesters. Development of new sensitive substrates. Journal of Biological Chemistry. ,vol. 256, pp. 12362- 12366 ,(1981) , 10.1016/S0021-9258(18)43280-2
M Poe, J T Blake, D A Boulton, M Gammon, N H Sigal, J K Wu, H J Zweerink, Human cytotoxic lymphocyte granzyme B. Its purification from granules and the characterization of substrate and inhibitor specificity. Journal of Biological Chemistry. ,vol. 266, pp. 98- 103 ,(1991) , 10.1016/S0021-9258(18)52407-8
G L Kucera, C Miller, P J Sisson, R W Wilcox, Z Wiemer, M Waite, Hydrolysis of thioester analogs by rat liver phospholipase A1. Journal of Biological Chemistry. ,vol. 263, pp. 12964- 12969 ,(1988) , 10.1016/S0021-9258(18)37657-9
Chih-Min Kam, J. C. Powers, U. Winkler, D. Hudig, N. J. Allison, T. M. Pickett, The function of lymphocyte proteases. Inhibition and restoration of granule-mediated lysis with isocoumarin serine protease inhibitors. Journal of Immunology. ,vol. 147, pp. 1360- 1368 ,(1991)