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DBH-like monooxygenase protein 1, also known as monooxygenase X, is an enzyme that in humans is encoded by the MOXD1gene.[5][6]
DBH-like 1 maintains many of the structural features of dopamine beta-monooxygenaseDBH.[7] Since Peptidylglycine alpha-hydroxylating monooxygenase (PHM; EC 1.14.17.3) is homologous to dopamine beta-monooxygenase (DBM; EC 1.14.17.1)[8] this concerns a structural basis for a new family of copper type II, significantly specific for ascorbate-dependent monooxygenases[8] based on the corresponding mouse homolog.[6] The pathway of catecholamine synthesis is a possible catecholamine-binding metabolic copper[9] enzyme domain, a neuron-like property encoding MOX without a signal sequence enzyme metabolism resolving the monooxygenase X chemical pathway[9] of an unknown substrate,[6]exogenous MOX is not secreted, and it localizes throughout the endoplasmic reticulum,[9] in both endocrine or nonendocrine cells.[9]
Deficiency
DBH deficiency has been treated effectively with L-threo-3,4-dihydroxyphenylserine (DOPS).[10]
^ abcChambers KJ, Tonkin LA, Chang E, Shelton DN, Linskens MH, Funk WD (September 1998). "Identification and cloning of a sequence homologue of dopamine beta-hydroxylase". Gene. 218 (1–2): 111–20. doi:10.1016/S0378-1119(98)00344-8. PMID9751809.
^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. ISSN1420-682X. PMID11028916.
^ abSouthan 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. PMID2792366.
^ abcdXin 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. PMID15337741.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^Vincent S, Robertson D (May 2002). "The broader view: catecholamine abnormalities". Clin Auton Res. Suppl. 1: 144–9. ISSN0959-9851. PMID12102462.
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. PMID15337741.{{cite journal}}: CS1 maint: unflagged free DOI (link)
