| IED ID | IndEnz0002019367 |
| Enzyme Type ID | protease019367 |
| Protein Name |
Bleomycin hydrolase BH BLM hydrolase BMH EC 3.4.22.40 |
| Gene Name | Blmh |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MNNAGLNSEKVAALIQKLNSDPQFVLAQNVGTTHDLLDICLKRATVQGAQHVFQHVVPQEGKPVTNQKSSGRCWIFSCLNVMRLPFMKKFNIEEFEFSQSYLFFWDKVERCYFFLNAFVDTAQKKEPEDGRLVQYLLMNPTNDGGQWDMLVNIVEKYGVVPKKCFPESHTTEATRRMNDILNHKMREFCIRLRNLVHSGATKGEISSTQDAMMEEIFRVVCICLGNPPETFTWEYRDKDKNYHKVGPITPLQFYKEHVKPLFNMEDKICFVNDPRPQHKYNKLYTVDYLSNMVGGRKTLYNNQPIDFLKKMVAASIRDGEAVWFGCDVGKHFNGKLGLSDMNVYDHELVFGVSLKNMNKAERLAFGESLMTHAMTFTAVSEKDDQEGAFVKWRVENSWGEDHGHKGYLCMTDEWFSEYVYEVVVDKKHVPEEVLAVLEQEPIVLPAWDPMGALA |
| Enzyme Length | 454 |
| Uniprot Accession Number | P70645 |
| 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 (By similarity). Binds single-stranded DNA with higher affinity than double-stranded DNA. May play an important role in the metabolism of antibiotics. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Modified residue (2) |
| Keywords | Acetylation;Cytoplasm;Direct protein sequencing;Hydrolase;Protease;Reference proteome;Thiol protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13867}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q13867}. Note=Co-localizes with NUDT12 in the cytoplasmic granules. {ECO:0000250|UniProtKB:Q13867}. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000269|PubMed:8907172; MOD_RES 391; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q13867 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16396496; 16472072; 17158865; |
| Motif | |
| Gene Encoded By | |
| Mass | 52,323 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.40; |