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MOXD1
Identifiers
Aliases	MOXD1, MOX, PRO5780, dJ248E1.1, Monooxygenase DBH-like 1, monooxygenase DBH like 1
External IDs	OMIM: 609000; MGI: 1921582; HomoloGene: 22904; GeneCards: MOXD1; OMA:MOXD1 - orthologs
Gene location (Human) Chr. Chromosome 6 (human) Band 6q23.2 Start 132,296,055 bp End 132,401,475 bp
Gene location (Mouse) Chr. Chromosome 10 (mouse) Band 10|10 A4 Start 24,099,415 bp End 24,178,688 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ventricular zone ganglionic eminence cartilage tissue periodontal fiber gallbladder body of uterus stromal cell of endometrium gastric mucosa myometrium left adrenal gland Top expressed in vas deferens lumbar spinal ganglion Epithelium of choroid plexus lip hair follicle skin of external ear molar sciatic nerve external carotid artery efferent ductule More reference expression data BioGPS n/a
Gene ontology Molecular function monooxygenase activity oxidoreductase activity protein binding catalytic activity metal ion binding copper ion binding dopamine beta-monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen Cellular component integral component of membrane endoplasmic reticulum membrane endoplasmic reticulum membrane extracellular space secretory granule membrane cytoplasm Biological process octopamine biosynthetic process dopamine catabolic process norepinephrine biosynthetic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 26002 59012 Ensembl ENSG00000079931 ENSMUSG00000020000 UniProt Q6UVY6 Q9CXI3 RefSeq (mRNA) NM_015529 NM_021509 RefSeq (protein) NP_056344 NP_067484 Location (UCSC) Chr 6: 132.3 – 132.4 Mb Chr 10: 24.1 – 24.18 Mb PubMed search
Wikidata
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DBH-like monooxygenase protein 1, also known as monooxygenase X, is an enzyme that in humans is encoded by the MOXD1 gene.

DBH-like 1 maintains many of the structural features of dopamine beta-monooxygenase DBH. Since Peptidylglycine alpha-hydroxylating monooxygenase (PHM; EC 1.14.17.3) is homologous to dopamine beta-monooxygenase (DBM; EC 1.14.17.1) this concerns a structural basis for a new family of copper type II, significantly specific for ascorbate-dependent monooxygenases based on the corresponding mouse homolog. The pathway of catecholamine synthesis is a possible catecholamine-binding metabolic copper enzyme domain, a neuron-like property encoding MOX without a signal sequence enzyme metabolism resolving the monooxygenase X chemical pathway of an unknown substrate, exogenous MOX is not secreted, and it localizes throughout the endoplasmic reticulum, in both endocrine or nonendocrine cells.

Deficiency

DBH deficiency has been treated effectively with L-threo-3,4-dihydroxyphenylserine (DOPS).

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

1. ^ GRCh38: Ensembl release 89: ENSG00000079931 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000020000 – 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.
5. "Entrez Gene: monooxygenase, DBH-like 1".
6. ^ 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.
7. 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.
8. ^ 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.
9. ^ 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.
10. 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.

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