| IED ID | IndEnz0002018897 |
| Enzyme Type ID | protease018897 |
| Protein Name |
Bleomycin hydrolase BH BLM hydrolase BMH EC 3.4.22.40 Aminopeptidase H |
| Gene Name | BLMH |
| Organism | Gallus gallus (Chicken) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Neognathae Galloanserae Galliformes Phasianidae (turkeys) Phasianinae Gallus Gallus gallus (Chicken) |
| Enzyme Sequence | MNAHGLSTEKAAAFTRRLRAEPQFLLAQNVATCSDPLEVCLQRQVVQDTIQVFQHAVPAEGKPVTNQKNSGRCWIFSCLNAMRLPFMKKYNIEEFEFSQSYLFFWDKVERCYYFLNAFVETAQKKEPIDGRLVQFLLTNPTNDGGQWDMLVNIVEKYGVVPKKYFPESHTTEATRRMNEILNHKMREYCLRLRNMVATGTNKEELCAAMDTMIEEVFRIVSTCLGNPPETFCWEFRDKEKNYHKFGPMTPVQFYNEHVKPYFNMEDKVCLVNDPRPQNPYCQLYTVEYLGNMAGGRKTLYNNQPIEVLKKLAATSIKDGEAVWFGCDVAKHFYSKLGINDLNIFNHELVFGVSVKNMNKAERLIFGDSLMTHAMVLTAVSEKDGQEDCYEKWRVENSWGEDRGNKGYLIMTDDWFSEYVYEVVVDKKYVPEDVLAVMEQEPIVLPAWDPMGALAK |
| Enzyme Length | 455 |
| Uniprot Accession Number | P87362 |
| Absorption | |
| Active Site | ACT_SITE 73; /evidence=ECO:0000255|PROSITE-ProRule:PRU10088; ACT_SITE 372; /evidence=ECO:0000255|PROSITE-ProRule:PRU10088; ACT_SITE 396; /evidence=ECO:0000255|PROSITE-ProRule:PRU10088 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=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.; EC=3.4.22.40; |
| DNA Binding | |
| EC Number | 3.4.22.40 |
| Enzyme Function | FUNCTION: The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B-aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1) |
| Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Protease;Reference proteome;Thiol protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13867}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 52,690 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |