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ENZYME entry: EC 220.127.116.11
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|Aminopeptidase C (Lactococcus lactis).|
|Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by hydrolysis of a carboxyamide bond of beta-aminoalanine, but also shows general aminopeptidase activity. The specificity varies somewhat with source, but amino acid arylamides of Met, Leu and Ala are preferred|
- The active sites are on the walls of a central channel through the
molecule, and access of substrate molecules to them is obstructed by
this and by the C-terminus of each polypeptide chain.
- Bleomycin can scarcely be the natural substrate, and there are
reports of limited endopeptidase activity.
- Known from bacteria as well as eukaryotic organisms.
- Hydrolase H from chicken muscle has many similarities to bleomycin
hydrolase, but hydrolyzes Ph-CO-Arg-2-naphthylamine as well as
- Belongs to peptidase family C1.
|PRIAM enzyme-specific profiles||18.104.22.168|
|KEGG Ligand Database for Enzyme Nomenclature||22.214.171.124|
|IUBMB Enzyme Nomenclature||126.96.36.199|
|MEDLINE||Find literature relating to 188.8.131.52|
|B3LP78, BLH1_YEAS1; ||C7GPC1, BLH1_YEAS2; ||B5VQH0, BLH1_YEAS6; |
|A6ZRK4, BLH1_YEAS7; ||C8ZFZ7, BLH1_YEAS8; ||Q01532, BLH1_YEAST; |
|P87362, BLMH_CHICK; ||Q13867, BLMH_HUMAN; ||Q8R016, BLMH_MOUSE; |
|P13019, BLMH_RABIT; ||P70645, BLMH_RAT; ||Q48543, PEPC_LACDL; |
|Q10744, PEPC_LACHE; ||Q9CEG3, PEPC_LACLA; ||Q04723, PEPC_LACLC; |
|Q928V0, PEPC_LISIN; ||O69192, PEPC_LISMO; ||Q56115, PEPC_STRTR; |
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