|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 22.214.171.124
Supersedes EC number: 126.96.36.199
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, 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: mucorpepsin
Enzyme Commission Synonyms: Mucor rennin, Mucor acid proteinase, Mucor acid protease, Mucor miehei aspartic proteinase, Mucor miehei aspartic protease, Mucor aspartic proteinase, Mucor pusillus emporase, Fromase 100, Mucor pusillus rennin, Fromase 46TL, Mucor miehei rennin
Taxonomic Range: Fungi
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): 36.144756 [Latendresse13]
Enzyme Commission Summary:
This enzyme catalyzes hydrolysis of proteins, favouring hydrophobic residues at P1 and P1'. Clots milk. Does not accept Lys at P1, and hence does not activate trypsinogen.
Isolated from the zygomycete fungi Mucor pusillus and M. miehei. The two species variants show 83% sequence identity and are immunologically crossreactive. In peptidase family A1 (pepsin A family). Formerly included in EC 188.8.131.52
Baudys88: Baudys M, Foundling S, Pavlik M, Blundell T, Kostka V (1988). "Protein chemical characterization of Mucor pusillus aspartic proteinase. Amino acid sequence homology with the other aspartic proteinases, disulfide bond arrangement and site of carbohydrate attachment." FEBS Lett 235(1-2);271-4. PMID: 3042459
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