ExplorEnz: EC 3.4.21.37

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3.4.21.37

Accepted name:

leukocyte elastase

Reaction:

Hydrolysis of proteins, including elastin. Preferential cleavage Val┼ > Ala┼

Other name(s):

lysosomal elastase; neutrophil elastase; polymorphonuclear leukocyte elastase; elastase; elaszym; serine elastase; granulocyte elastase

Comments:

Differs from pancreatic elastase in specificity on synthetic substrates and in inhibitor sensitivity. In peptidase family S1 (trypsin family). Formerly included in EC 3.4.21.11

Links to other databases:

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

References:

1.	Barrett, A.J. Leukocyte elastase. Methods Enzymol. 80 (1981) 581–588. [PMID: 7043201]
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.	Stein, R.L., Strimpler, A.M., Hori, H. and Powers, J.C. Catalysis by human leukocyte elastase: mechanistic insights into specificity requirements. Biochemistry 26 (1987) 1301–1305. [PMID: 3646070]
4.	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 3.4.21.37 created 1981 (EC 3.4.4.7 created 1961, transferred 1972 to EC 3.4.21.11 created 1972, part incorporated 1984)]