Detail Information for IndEnz0002019367
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;