Bleomycin hydrolase

From Wikipedia, the free encyclopedia
(Redirected from BLMH)

Template:Short description Template:Cs1 config An Error has occurred retrieving Wikidata item for infobox Bleomycin hydrolase is an enzyme that in humans is encoded by the BLMH gene.[1][2][3]

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.[4] 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.[3]

Interactions

BLMH has been shown to interact with RPL29,[5] RPL11,[5] UBE2I[6] and Amyloid precursor protein.[7]

References

Page Template:Reflist/styles.css has no content.

  1. ^ Page Module:Citation/CS1/styles.css has no content.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.
  2. ^ Page Module:Citation/CS1/styles.css has no content.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.
  3. ^ a b Page Module:Citation/CS1/styles.css has no content."Entrez Gene: BLMH bleomycin hydrolase".
  4. ^ Page Module:Citation/CS1/styles.css has no content.Jarosław Zimny, Marta Sikora, Andrzej Guranowski, Hieronim Jakubowski (2006). "Protective Mechanisms against Homocysteine Toxicity". The Journal of Biological Chemistry. 281 (32): 22485–22492. Bibcode:2006JBiCh.28122485Z. doi:10.1074/jbc.M603656200. PMID 16769724.
  5. ^ a b Page Module:Citation/CS1/styles.css has no content.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.
  6. ^ Page Module:Citation/CS1/styles.css has no content.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.
  7. ^ Page Module:Citation/CS1/styles.css has no content.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.

Further reading

Page Template:Refbegin/styles.css has no content.

Lua error in package.lua at line 80: module 'Module:Navbox/configuration' not found. Lua error in package.lua at line 80: module 'Module:Navbox/configuration' not found. Lua error in package.lua at line 80: module 'Module:Navbox/configuration' not found. Lua error in mw.title.lua at line 404: bad argument #2 to 'title.new' (unrecognized namespace name 'Portal').


Template:Asbox