The Enzyme Database

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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 name(s): 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 endopeptidase from Uca pugilator [4], digestive enzymes from other decapod crustacea [5,6], and an enzyme from the fungus Entomophthora coronata [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 848900-32-3
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. [DOI] [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. [DOI] [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 created 1978]

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