Brachyurin - Misplaced Pages

Brachyurin (EC 3.4.21.32, Uca pugilator collagenolytic proteinase, crab protease I, crab protease II) is an enzyme. 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

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.
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.
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.
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.
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.
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.

External links

Brachyurin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21)
Digestive enzymes	Enteropeptidase Trypsin Chymotrypsin Elastase Neutrophil Pancreatic
Coagulation	factors: Thrombin Factor VIIa Factor IXa Factor Xa Factor XIa Factor XIIa Kallikrein PSA KLK1 KLK2 KLK3 KLK4 KLK5 KLK6 KLK7 KLK8 KLK9 KLK10 KLK11 KLK12 KLK13 KLK14 KLK15 fibrinolysis: Plasmin Plasminogen activator Tissue plasminogen activator Urinary plasminogen activator
Complement system	Factor B Factor D Factor I MASP MASP1 MASP2 C3-convertase
Other immune system	Chymase Granzyme Tryptase Proteinase 3/Myeloblastin
Venombin	Ancrod Batroxobin
Other	Acrosin Prolyl endopeptidase Pronase Proprotein convertases 1 2 Prostasin Reelin Subtilisin/Furin/S1P4 Sedolisin/TPP1 Streptokinase Cathepsin A G

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

Category:

EC 3.4.21