Bleomycin hydrolase is an enzyme that in humans is encoded by the BLMH gene.[5][6][7]

BLMH
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesBLMH, BH, BMH, bleomycin hydrolase
External IDsOMIM: 602403; MGI: 1345186; HomoloGene: 330; GeneCards: BLMH; OMA:BLMH - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000386

NM_178645

RefSeq (protein)

NP_000377

NP_848760

Location (UCSC)Chr 17: 30.25 – 30.29 MbChr 11: 76.82 – 76.88 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Bleomycin hydrolase (BMH) is a cytoplasmic cysteine peptidase that is highly conserved through evolution. Its biological function is hydrolysis of the reactive electrophile homocysteine thiolactone.[8] Another of its activities is metabolic inactivation of the glycopeptide bleomycin (BLM), an essential component of combination chemotherapy regimens for cancer. The protein contains the signature active site residues of the cysteine protease papain superfamily.[7]

Interactions

edit

BLMH has been shown to interact with RPL29,[9] RPL11,[9] UBE2I[10] and Amyloid precursor protein.[11]

References

edit
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000108578Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020840Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Ferrando AA, Pendas AM, Llano E, Velasco G, Lidereau R, Lopez-Otin C (January 1998). "Gene characterization, promoter analysis, and chromosomal localization of human bleomycin hydrolase". J Biol Chem. 272 (52): 33298–304. doi:10.1074/jbc.272.52.33298. PMID 9407121.
  6. ^ Montoya SE, Ferrell RE, Lazo JS (October 1997). "Genomic structure and genetic mapping of the human neutral cysteine protease bleomycin hydrolase". Cancer Res. 57 (19): 4191–5. PMID 9331073.
  7. ^ a b "Entrez Gene: BLMH bleomycin hydrolase".
  8. ^ Jarosław Zimny, Marta Sikora, Andrzej Guranowski, Hieronim Jakubowski (2006). "Protective Mechanisms against Homocysteine Toxicity". The Journal of Biological Chemistry. 281 (32): 22485–22492. doi:10.1074/jbc.M603656200. PMID 16769724.
  9. ^ a b Koldamova RP, Lefterov I M, DiSabella M T, Almonte C, Watkins S C, Lazo J S (June 1999). "Human bleomycin hydrolase binds ribosomal proteins". Biochemistry. 38 (22). UNITED STATES: 7111–7. doi:10.1021/bi990135l. ISSN 0006-2960. PMID 10353821.
  10. ^ Koldamova RP, Lefterov I M, DiSabella M T, Lazo J S (December 1998). "An evolutionarily conserved cysteine protease, human bleomycin hydrolase, binds to the human homologue of ubiquitin-conjugating enzyme 9". Mol. Pharmacol. 54 (6). UNITED STATES: 954–61. doi:10.1124/mol.54.6.954. ISSN 0026-895X. PMID 9855622. S2CID 2272861.
  11. ^ Lefterov IM, Koldamova R P, Lazo J S (September 2000). "Human bleomycin hydrolase regulates the secretion of amyloid precursor protein". FASEB J. 14 (12). UNITED STATES: 1837–47. doi:10.1096/fj.99-0938com. ISSN 0892-6638. PMID 10973933. S2CID 44302063.
edit

Further reading

edit