MetaCyc Reaction:

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

EC Number:

Supersedes EC number:

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: The left side is missing: Peptides: 2 . The right side is missing: Proteins: 1 O: 1 H: 1

Enzyme Commission Primary Name: clostripain

Enzyme Commission Synonyms: clostridiopeptidase B, clostridium histolyticum proteinase B, α-clostridipain, clostridiopeptidase

Taxonomic Range: Bacteria

Standard Gibbs Free Energy (ΔrG in kcal/mol): 36.144756Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
This enzyme catalyzes preferential cleavege :Arg-|-, including Arg-|-Pro, but not Lys-.

From the bacterium Clostridium histolytic . It requires Ca2+ ions and is inhibited by EDTA. Type example of peptidase family.

Citations: [Mitchell77, Gilles79, Gilles84]

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:, UniProt:RELATED-TO:P09870


Gilles79: Gilles AM, Imhoff JM, Keil B (1979). "alpha-Clostripain. Chemical characterization, activity, and thiol content of the highly active form of clostripain." J Biol Chem 254(5);1462-8. PMID: 762145

Gilles84: Gilles AM, Lecroisey A, Keil B (1984). "Primary structure of alpha-clostripain light chain." Eur J Biochem 145(3);469-76. PMID: 6391922

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Mitchell77: Mitchell WM (1977). "Cleavage at arginine residues by clostripain." Methods Enzymol 47;165-70. PMID: 927173

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 Mon Nov 30, 2015, BIOCYC14A.