IUBMB Enzyme Nomenclature

EC 3.4.21.32

Accepted name: brachyurin

Reaction: Hydrolysis of proteins, with broad specificity for peptide bonds. Native collagen is cleaved about 75% of the length of the molecule from the N-terminus. Low activity on small molecule substrates of both trypsin and chymotrypsin

Other names: Uca pugilator collagenolytic proteinase; crab protease I; crab protease II

Comments: From hepatopancreas of the fiddler crab, Uca pugilator. In peptidase family S1 (trypsin family). Other serine endopeptidases that degrade collagen, but are not listed separately here, include a second endopeptidases from Uca pugilator [4], digestive enzymes from other decapod crustacea [5,6], and an enzyme from the fungus Entomophthora coronata (formerly EC 3.4.21.33) [1]

Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 848900-32-3

References

1. Hurion, N., Fromentin, H. and Keil, B. Specificity of the collagenolytic enzyme from the fungus Entomophthora coronata: comparison with the bacterial collagenase from Achromobacter iophagus. Arch. Biochem. Biophys. 192 (1979) 438-445. [PMID: 219780]

2. Grant, G.A., Eisen, A.Z. and Bradshaw, R.A. Collagenolytic protease from fiddler crab (Uca pugilator). Methods Enzymol. 80 (1981) 722-734

3. Welgus, H.G., Grant, G.A., Jeffrey, J.J. and Eisen, A.Z. Substrate specificity of the collagenolytic serine protease from Uca pugilator: studies with collagenous substrates. Biochemistry 21 (1982) 5183-5189. [PMID: 6756469]

4. Welgus, H.G. and Grant, G.A. Degradation of collagen substrates by a trypsin-like serine protease form the fiddler crab Uca pugilator. Biochemistry 22 (1983) 2228-2233. [PMID: 6305411]

5. Klimova, O.A., Borukhov, S.I., Solovyeva, N.I., Balaevskaya, T.O. and Strongin, A.Y. The isolation and properties of collagenolytic proteases from crab hepatopancreas. Biochem. Biophys. Res. Commun. 166 (1990) 1411-1420. [PMID: 2154979]

6. Lu, P.-J., Liu, H.-C. and Tsai, I.-H. The midgut trypsins of shrimp (Penaeus monodon). High efficiency toward native protein substrates including collagens. Biol. Chem. Hoppe-Seyler 371 (1990) 851-859. [PMID: 1963309]

[EC 3.4.21.32 created 1978]


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