ExplorEnz: EC 3.4.21.36

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3.4.21.36

Accepted name:

pancreatic elastase

Reaction:

Hydrolysis of proteins, including elastin. Preferential cleavage: Ala┼

Other name(s):

pancreatopeptidase E; pancreatic elastase I; elastase; elaszym; serine elastase

Comments:

Formed by activation of proelastase from mammalian pancreas by trypsin. In peptidase family S1 (trypsin family). Formerly included in EC 3.4.21.11

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9004-06-2

References:

1.	Shotton, D.M. Elastase. Methods Enzymol. 19 (1970) 113–140.
2.	Harper, J.W., Cook, R.R., Roberts, C.J., McLaughlin, B.J. and Powers, J.C. Active site mapping of the serine proteases human leukocyte elastase, cathepsin G, porcine pancreatic elastase, rat mast cell proteases I and II, bovine chymotrypsin Aα, and Staphylococcus aureus protease V-8 using tripeptide thiobenzyl ester substrates. Biochemistry 23 (1984) 2995–3002. [PMID: 6380580]
3.	Kawashima, I., Tani, T., Shimoda, K. and Takiguchi, Y. Characterization of pancreatic elastase II cDNAs: two elastase II mRNAs are expressed in human pancreas. DNA 6 (1987) 163–172. [DOI] [PMID: 3646943]
4.	Bieth, J.G., Dirrig, S., Jung, M.-L., Boudier, C., Papamichael, E., Sakarellos, C. and Dimicoli, J.-L. Investigation of the active center of rat pancreatic elastase. Biochim. Biophys. Acta 994 (1989) 64–74. [DOI] [PMID: 2909256]
5.	Bode, W., Meyer, E., Jr. and Powers, J.C. Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors. Biochemistry 28 (1989) 1951–1963. [PMID: 2655701]

[EC 3.4.21.36 created 1981 (EC 3.4.4.7 created 1961, transferred 1972 to EC 3.4.21.11 created 1972, part incorporated 1984)]