Bleomycin hydrolase

BLMH
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1CB5, 2CB5
Identifiers
Aliases	BLMH, BH, BMH, bleomycin hydrolase
External IDs	OMIM: 602403 MGI: 1345186 HomoloGene: 330 GeneCards: BLMH
Gene location (Human)
Chr.	Chromosome 17 (human)
End	30,292,056 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	76,878,205 bp
RNA expression pattern
	Top expressed in
	skin of abdomen; ; body of pancreas; ; stromal cell of endometrium; ; islet of Langerhans; ; ascending aorta; ; vulva; ; gastrocnemius muscle; ; right coronary artery; ; ganglionic eminence; ; left coronary artery;
	Top expressed in
	fossa; ; condyle; ; primitive streak; ; hair follicle; ; renal corpuscle; ; internal carotid artery; ; esophagus; ; vas deferens; ; external carotid artery; ; skin of abdomen;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	peptidase activity; hydrolase activity; carboxypeptidase activity; cysteine-type endopeptidase activity; protein binding; cysteine-type peptidase activity; aminopeptidase activity; identical protein binding;
Cellular component	extracellular exosome; cytosol; nucleus; cytoplasm;
Biological process	protein polyubiquitination; proteolysis; response to toxic substance; homocysteine catabolic process;
	Sources:Amigo / QuickGO
Orthologs
	642
	104184
	ENSG00000108578
	ENSMUSG00000020840
	Q13867
	Q8R016
	NM_000386
	NM_178645
	NP_000377
	NP_848760
	Wikidata
View/Edit Human	View/Edit Mouse

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

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

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

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000108578 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020840 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
↑ 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.
1 2 "Entrez Gene: BLMH bleomycin hydrolase".
↑ 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.
1 2 Koldamova, R P; Lefterov I M; DiSabella M T; Almonte C; Watkins S C; Lazo J S (June 1999). "Human bleomycin hydrolase binds ribosomal proteins". Biochemistry. UNITED STATES. 38 (22): 7111–7. doi:10.1021/bi990135l. ISSN 0006-2960. PMID 10353821.
↑ Koldamova, R P; 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. UNITED STATES. 54 (6): 954–61. doi:10.1124/mol.54.6.954. ISSN 0026-895X. PMID 9855622. S2CID 2272861.
↑ Lefterov, I M; Koldamova R P; Lazo J S (September 2000). "Human bleomycin hydrolase regulates the secretion of amyloid precursor protein". FASEB J. UNITED STATES. 14 (12): 1837–47. doi:10.1096/fj.99-0938com. ISSN 0892-6638. PMID 10973933. S2CID 44302063.

External links

Human BLMH genome location and BLMH gene details page in the UCSC Genome Browser.
Overview of all the structural information available in the PDB for UniProt: Q13867 (Bleomycin hydrolase) at the PDBe-KB.

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Ferrando AA, Velasco G, Campo E, Lopez-Otin C (1996). "Cloning and expression analysis of human bleomycin hydrolase, a cysteine proteinase involved in chemotherapy resistance". Cancer Res. 56 (8): 1746–50. PMID 8620487.
Brömme D, Rossi AB, Smeekens SP, et al. (1996). "Human bleomycin hydrolase: molecular cloning, sequencing, functional expression, and enzymatic characterization". Biochemistry. 35 (21): 6706–14. doi:10.1021/bi960092y. PMID 8639621.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Koldamova RP, Lefterov IM, Gadjeva VG, Lazo JS (1998). "Essential binding and functional domains of human bleomycin hydrolase". Biochemistry. 37 (8): 2282–90. doi:10.1021/bi9722204. PMID 9485374.
Montoya SE, Aston CE, DeKosky ST, et al. (1998). "Bleomycin hydrolase is associated with risk of sporadic Alzheimer's disease". Nat. Genet. 18 (3): 211–2. doi:10.1038/ng0398-211. PMID 9500538. S2CID 2940414.
Zheng W, Johnston SA, Joshua-Tor L (1998). "The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase". Cell. 93 (1): 103–9. doi:10.1016/S0092-8674(00)81150-2. PMID 9546396.
Koldamova RP, Lefterov IM, DiSabella MT, Lazo JS (1999). "An evolutionarily conserved cysteine protease, human bleomycin hydrolase, binds to the human homologue of ubiquitin-conjugating enzyme 9". Mol. Pharmacol. 54 (6): 954–61. doi:10.1124/mol.54.6.954. PMID 9855622. S2CID 2272861.
Takeda A, Nonaka M, Ishikawa A, Higuchi D (1999). "Immunohistochemical localization of the neutral cysteine protease bleomycin hydrolase in human skin". Arch. Dermatol. Res. 291 (4): 238–40. doi:10.1007/s004030050400. PMID 10335922. S2CID 10799259.
Koldamova RP, Lefterov IM, DiSabella MT, et al. (1999). "Human bleomycin hydrolase binds ribosomal proteins". Biochemistry. 38 (22): 7111–7. doi:10.1021/bi990135l. PMID 10353821.
O'Farrell PA, Gonzalez F, Zheng W, et al. (1999). "Crystal structure of human bleomycin hydrolase, a self-compartmentalizing cysteine protease". Structure. 7 (6): 619–27. doi:10.1016/S0969-2126(99)80083-5. PMID 10404591.
Malherbe P, Faull RL, Richards JG (2000). "Regional and cellular distribution of bleomycin hydrolase mRNA in human brain: comparison between Alzheimer's diseased and control brains". Neurosci. Lett. 281 (1): 37–40. doi:10.1016/S0304-3940(00)00802-8. PMID 10686410. S2CID 41562274.
Lefterov IM, Koldamova RP, Lazo JS (2000). "Human bleomycin hydrolase regulates the secretion of amyloid precursor protein". FASEB J. 14 (12): 1837–47. doi:10.1096/fj.99-0938com. PMID 10973933. S2CID 44302063.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Nivet-Antoine V, Coulhon MP, Le Denmat C, et al. (2003). "[Apolipoprotein E and bleomycin hydrolase. Polymorphisms: association with neurodegenerative diseases]". Ann. Biol. Clin. (Paris). 61 (1): 61–7. PMID 12604387.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000108578 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020840 - Ensembl, 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.

[pmid9407121-5] 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.

[pmid9331073-6] 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.

[entrez-7] 1 2 "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.

[pmid10353821-9] 1 2 Koldamova, R P; Lefterov I M; DiSabella M T; Almonte C; Watkins S C; Lazo J S (June 1999). "Human bleomycin hydrolase binds ribosomal proteins". Biochemistry. UNITED STATES. 38 (22): 7111–7. doi:10.1021/bi990135l. ISSN 0006-2960. PMID 10353821.

[pmid9855622-10] Koldamova, R P; 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. UNITED STATES. 54 (6): 954–61. doi:10.1124/mol.54.6.954. ISSN 0026-895X. PMID 9855622. S2CID 2272861.

[pmid10973933-11] Lefterov, I M; Koldamova R P; Lazo J S (September 2000). "Human bleomycin hydrolase regulates the secretion of amyloid precursor protein". FASEB J. UNITED STATES. 14 (12): 1837–47. doi:10.1096/fj.99-0938com. ISSN 0892-6638. PMID 10973933. S2CID 44302063.

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Proteases: cysteine proteases (EC 3.4.22)
Caspase	Caspase 1 Caspase 2 Caspase 3 Caspase 4 Caspase 5 Caspase 6 Caspase 7 Caspase 8 Caspase 9 Caspase 10 Caspase 12 Caspase 13 Caspase 14
Fruit-derived	Papain Ficain Bromelain Actinidain
Calpain	CAPN1 CAPN2 CAPN3 CAPN5 CAPN6 CAPN7 CAPN8 CAPN9 CAPN10 CAPN11 CAPN12 CAPN13 CAPN14 CAPNS1 CAPNS2
Cathepsin	B C F H K L1/L2 O S W Z
Other	Clostripain Cancer procoagulant Separase Autophagin Cruzipain 3C-like protease Gingipain R Gingipain K

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Interactions

References

External links

Further reading