Monooxygenase DBH-like 1
An Error has occurred retrieving Wikidata item for infobox DBH-like monooxygenase protein 1, also known as monooxygenase X, is an enzyme that in humans is encoded by the MOXD1 gene.[1][2] DBH-like 1 maintains many of the structural features of dopamine beta-monooxygenase DBH.[3] Since Peptidylglycine alpha-hydroxylating monooxygenase (PHM; EC 1.14.17.3) is homologous to dopamine beta-monooxygenase (DBM; EC 1.14.17.1)[4] this concerns a structural basis for a new family of copper type II, significantly specific for ascorbate-dependent monooxygenases[4] based on the corresponding mouse homolog.[2] The pathway of catecholamine synthesis is a possible catecholamine-binding metabolic copper[5] enzyme domain, a neuron-like property encoding MOX without a signal sequence enzyme metabolism resolving the monooxygenase X chemical pathway[5] of an unknown substrate,[2] exogenous MOX is not secreted, and it localizes throughout the endoplasmic reticulum,[5] in both endocrine or nonendocrine cells.[5]
Deficiency
DBH deficiency has been treated effectively with L-threo-3,4-dihydroxyphenylserine (DOPS).[6]
See also
- Dopamine-beta-hydroxylase-DBH,
- Dopamine beta-monooxygenase-DBM,
- Peptidylglycine alpha-hydroxylating monooxygenase-PHM
- peptidyl-alpha-hydroxyglycine alpha-amidating lyase-PAL
- Tyrosine 3-monooxygenase-TH.
References
- ↑ "Entrez Gene: monooxygenase, DBH-like 1".
- ↑ 2.0 2.1 2.2 Chambers KJ, Tonkin LA, Chang E, Shelton DN, Linskens MH, Funk WD (September 1998). "Identification and cloning of a sequence homologue of dopamine beta-hydroxylase" (PDF). Gene. 218 (1–2): 111–20. doi:10.1016/S0378-1119(98)00344-8. PMID 9751809.
- ↑ Prigge ST, Mains RE, Eipper BA, Amzel LM (August 2000). "New insights into copper monooxygenases and peptide amidation: structure, mechanism and function". Cell Mol Life Sci. 57 (8–9): 1236–59. doi:10.1007/PL00000763. ISSN 1420-682X. PMC 11146793. PMID 11028916. S2CID 12738480.
- ↑ 4.0 4.1 Southan C, Kruse LI (September 1989). "Sequence similarity between dopamine beta-hydroxylase and peptide alpha-amidating enzyme: evidence for a conserved catalytic domain". FEBS Lett. 255 (1): 116–20. doi:10.1016/0014-5793(89)81072-5. PMID 2792366. S2CID 84464131.
- ↑ 5.0 5.1 5.2 5.3 Xin X, Mains RE, Eipper BA (November 2004). "Monooxygenase X, a member of the copper-dependent monooxygenase family localized to the endoplasmic reticulum". J. Biol. Chem. 279 (46): 48159–67. doi:10.1074/jbc.M407486200. PMID 15337741.
- ↑ Vincent S, Robertson D (May 2002). "The broader view: catecholamine abnormalities". Clin Auton Res. Suppl. 1 (7): 144–9. doi:10.1007/s102860200018. ISSN 0959-9851. PMID 12102462. S2CID 28678929.
Further reading
- Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
- Xin X, Mains RE, Eipper BA (2004). "Monooxygenase X, a member of the copper-dependent monooxygenase family localized to the endoplasmic reticulum". J. Biol. Chem. 279 (46): 48159–67. doi:10.1074/jbc.M407486200. PMID 15337741.
- Bon S, Lamouroux A, Vigny A, Massoulié J, Mallet J, Henry JP (October 1991). "Amphiphilic and nonamphiphilic forms of bovine and human dopamine beta-hydroxylase". J. Neurochem. 57 (4): 1100–11. doi:10.1111/j.1471-4159.1991.tb08267.x. ISSN 0022-3042. PMID 1654385. S2CID 85087782.
