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MetaCyc Reaction: 3.4.24.48

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number: 3.4.24.48

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

Mass balance status: Balance undetermined; a substrate has a non-numerical coefficient

Enzyme Commission Primary Name: ruberlysin

Enzyme Commission Synonyms: Crotalus ruber metalloendopeptidase II, hemorrhagic toxin II

Taxonomic Range: Metazoa

Enzyme Commission Summary:
This enzyme catalyzes cleavage of His10-|-Leu, Ala14-|-Leu, Tyr16-|-Leu and Gly23-|-Phe bonds in the B chain of insulin; His-|-Pro, Pro-|-Phe, and Trp-|-Ser of angiotensin I; and Gly-|-Phe of Met enkephalin.

A 25 kDa hemorrhagic endopeptidase from the venom of the red rattlesnake ( Crotalus ruber ruber) that cleaves fibrinogen. In peptidase family M12 (astacin family).

Citations: [Mori87, Takeya90]

Relationship Links: BRENDA:EC:3.4.24.48, ENZYME:EC:3.4.24.48, IUBMB-ExplorEnz:EC:3.4.24.48, UniProt:RELATED-TO:P20897


References

Mori87: Mori N, Nikai T, Sugihara H, Tu AT (1987). "Biochemical characterization of hemorrhagic toxins with fibrinogenase activity isolated from Crotalus ruber ruber venom." Arch Biochem Biophys 253(1);108-21. PMID: 2949699

Takeya90: Takeya H, Onikura A, Nikai T, Sugihara H, Iwanaga S (1990). "Primary structure of a hemorrhagic metalloproteinase, HT-2, isolated from the venom of Crotalus ruber ruber." J Biochem 108(5);711-9. PMID: 2081731


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.5 on Sun Feb 14, 2016, BIOCYC11A.