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Link to original content: https://en.wikipedia.org/wiki/Brachyurin
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Brachyurin

From Wikipedia, the free encyclopedia
Brachyurin
Identifiers
EC no.3.4.21.32
CAS no.848900-32-3
Databases
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BRENDABRENDA entry
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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

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  1. ^ Hurion N, Fromentin H, Keil B (February 1979). "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. doi:10.1016/0003-9861(79)90113-9. PMID 219780.
  2. ^ Grant GA, Eisen AZ, Bradshaw RA (1981). "Collagenolytic protease from fiddler crab (Uca pugilator)". Collagenolytic protease from fiddler crab (Uca pugilator). Methods Enzymol. Vol. 80. pp. 722–734. doi:10.1016/s0076-6879(81)80055-9. ISBN 978-0-12-181980-4.
  3. ^ Welgus HG, Grant GA, Jeffrey JJ, Eisen AZ (October 1982). "Substrate specificity of the collagenolytic serine protease from Uca pugilator: studies with collagenous substrates". Biochemistry. 21 (21): 5183–9. doi:10.1021/bi00264a012. PMID 6756469.
  4. ^ Welgus HG, Grant GA (April 1983). "Degradation of collagen substrates by a trypsin-like serine protease from the fiddler crab Uca pugilator". Biochemistry. 22 (9): 2228–33. doi:10.1021/bi00278a026. PMID 6305411.
  5. ^ Klimova OA, Borukhov SI, Solovyeva NI, Balaevskaya TO (February 1990). "The isolation and properties of collagenolytic proteases from crab hepatopancreas". Biochemical and Biophysical Research Communications. 166 (3): 1411–20. doi:10.1016/0006-291x(90)91024-m. PMID 2154979.
  6. ^ Lu PJ, Liu HC, Tsai IH (September 1990). "The midgut trypsins of shrimp (Penaeus monodon). High efficiency toward native protein substrates including collagens". Biological Chemistry Hoppe-Seyler. 371 (9): 851–9. doi:10.1515/bchm3.1990.371.2.851. PMID 1963309.
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