Biology:Brachyurin
From HandWiki
Brachyurin (EC 3.4.21.32, Uca pugilator collagenolytic proteinase, crab protease I, crab protease II) is an enzyme.[1][2][3][4][5][6] This enzyme catalyses the 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.
This enzyme is isolated from hepatopancreas of the fiddler crab, Uca pugilator.
References
- ↑ "Specificity of the collagenolytic enzyme from the fungus Entomophthora coronata: comparison with the bacterial collagenase from Achromobacter iophagus". Archives of Biochemistry and Biophysics 192 (2): 438–45. February 1979. doi:10.1016/0003-9861(79)90113-9. PMID 219780.
- ↑ "Collagenolytic protease from fiddler crab (Uca pugilator)". Methods Enzymol. 80: 722–734. 1981. doi:10.1016/s0076-6879(81)80055-9.
- ↑ "Substrate specificity of the collagenolytic serine protease from Uca pugilator: studies with collagenous substrates". Biochemistry 21 (21): 5183–9. October 1982. doi:10.1021/bi00264a012. PMID 6756469.
- ↑ "Degradation of collagen substrates by a trypsin-like serine protease from the fiddler crab Uca pugilator". Biochemistry 22 (9): 2228–33. April 1983. doi:10.1021/bi00278a026. PMID 6305411.
- ↑ "The isolation and properties of collagenolytic proteases from crab hepatopancreas". Biochemical and Biophysical Research Communications 166 (3): 1411–20. February 1990. doi:10.1016/0006-291x(90)91024-m. PMID 2154979.
- ↑ "The midgut trypsins of shrimp (Penaeus monodon). High efficiency toward native protein substrates including collagens". Biological Chemistry Hoppe-Seyler 371 (9): 851–9. September 1990. doi:10.1515/bchm3.1990.371.2.851. PMID 1963309.
External links
- Brachyurin at the US National Library of Medicine Medical Subject Headings (MeSH)
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