ExplorEnz: EC 3.4.21.59

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3.4.21.59

Accepted name:

tryptase

Reaction:

Preferential cleavage: Arg┼, Lys┼, but with more restricted specificity than trypsin

Other name(s):

mast cell tryptase; mast cell protease II; skin tryptase; lung tryptase; pituitary tryptase; mast cell neutral proteinase; mast cell serine proteinase II; mast cell proteinase II; mast cell serine proteinase tryptase; rat mast cell protease II; tryptase M

Comments:

Occurs as a tetrameric molecule with high affinity for heparin, in mast cell granules. In peptidase family S1 (trypsin family). Not inhibited by α₁-proteinase inhibitor or α2-macroglobulin

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 97501-93-4

References:

1.	Tanaka, T., McRae, B.J., Cho, K., Cook, R., Fraki, J.E., Johnson, D.A. and Powers, J.C. Mammalian tissue trypsin-like enzymes. Comparative reactivities of human skin tryptase, human lung tryptase, and bovine trypsin with peptide 4-nitroanilide and thioester substrates. J. Biol. Chem. 258 (1983) 13552–13557. [PMID: 6358206]
2.	Kido, H., Fukusen, N. and Katunuma, N. Chymotrypsin- and trypsin-type serine proteases in rat mast cells: properties and functions. Arch. Biochem. Biophys. 239 (1985) 436–443. [DOI] [PMID: 3890754]
3.	Cromlish, J.A., Seidah, N.G., Marcinkiewitz, M., Hamelin, J., Johnson, D.A. and Chrétien, M. Human pituitary tryptase: molecular forms, NH₂-terminal sequence, immunocytochemical localization, and specificity with prohormone and fluorogenic substrates. J. Biol. Chem. 262 (1987) 1363–1373. [PMID: 3543004]
4.	Harvima, I.T., Schechter, N.M., Harvima, R.J. and Fräki, J.E. Human skin tryptase: purification, partial characterization and comparison with human lung tryptase. Biochim. Biophys. Acta 957 (1988) 71–80. [DOI] [PMID: 3140898]
5.	Vanderslice, P., Ballinger, S.M., Tam, E.K., Goldstein, S.M., Craik, C.S. and Caughey, G. Human mast cell tryptase: multiple cDNAs and genes reveal a multigene serine protease family. Proc. Natl. Acad. Sci. USA 87 (1990) 3811–3815. [DOI] [PMID: 2187193]

[EC 3.4.21.59 created 1992]