Monooxygenase DBH-like 1 explained
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.
Further reading
- Clark HF, Gurney AL, Abaya E, etal . 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 . 2003 . 12975309 . 10.1101/gr.1293003 . 403697.
- Xin X, Mains RE, Eipper BA . Monooxygenase X, a member of the copper-dependent monooxygenase family localized to the endoplasmic reticulum. . J. Biol. Chem. . 279 . 46 . 48159–67 . 2004 . 15337741 . 10.1074/jbc.M407486200 . free .
- Bon S, Lamouroux A, Vigny A, Massoulié J, Mallet J, Henry JP . Amphiphilic and nonamphiphilic forms of bovine and human dopamine beta-hydroxylase. . J. Neurochem. . 57 . 4 . 1100–11 . October 1991 . 1654385 . 0022-3042. 10.1111/j.1471-4159.1991.tb08267.x. 85087782 .
Notes and References
- Web site: Entrez Gene: monooxygenase, DBH-like 1 .
- Chambers KJ, Tonkin LA, Chang E, Shelton DN, Linskens MH, Funk WD . Identification and cloning of a sequence homologue of dopamine beta-hydroxylase . Gene . 218 . 1–2 . 111–20 . September 1998 . 9751809 . 10.1016/S0378-1119(98)00344-8.
- Prigge ST, Mains RE, Eipper BA, Amzel LM . New insights into copper monooxygenases and peptide amidation: structure, mechanism and function. . Cell Mol Life Sci . 57 . 8–9 . 1236–59 . August 2000 . 11028916 . 1420-682X . 10.1007/PL00000763 . 12738480 . 11146793 .
- Southan C, Kruse LI . Sequence similarity between dopamine beta-hydroxylase and peptide alpha-amidating enzyme: evidence for a conserved catalytic domain. . FEBS Lett. . 255 . 1 . 116–20 . September 1989 . 2792366 . 10.1016/0014-5793(89)81072-5 . 84464131 .
- Xin X, Mains RE, Eipper BA . Monooxygenase X, a member of the copper-dependent monooxygenase family localized to the endoplasmic reticulum. . J. Biol. Chem. . 279 . 46 . 48159–67 . November 2004 . 15337741 . 10.1074/jbc.M407486200 . free .
- Vincent S, Robertson D . The broader view: catecholamine abnormalities. . Clin Auton Res . Suppl. 1 . 7. 144–9 . May 2002 . 12102462 . 10.1007/s102860200018. 28678929 . 0959-9851 .
