Monooxygenase DBH-like 1

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)
End	132,401,475 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	24,178,688 bp
RNA expression pattern
	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
	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
	26002
	59012
	ENSG00000079931
	ENSMUSG00000020000
	Q6UVY6
	Q9CXI3
	NM_015529
	NM_021509
	NP_056344
	NP_067484
	Wikidata
View/Edit Human	View/Edit Mouse

DBH-like monooxygenase protein 1, also known as monooxygenase X, is an enzyme that in humans is encoded by the MOXD1 gene.^[5]^[6]

DBH-like 1 maintains many of the structural features of dopamine beta-monooxygenase DBH.^[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]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000079931 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000020000 – 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.
^ "Entrez Gene: monooxygenase, DBH-like 1".
^ ^a ^b ^c 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.
^ ^a ^b 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.
^ ^a ^b ^c ^d 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.

v t e Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)
1.14.11: 2-oxoglutarate	Prolyl hydroxylase HIF prolyl-hydroxylase EGLN1 EGLN2 EGLN3 P4HTM Lysyl hydroxylase AlkB ALKBH1 FTO
1.14.13: NADH or NADPH	Flavin-containing monooxygenase FMO1 FMO2 FMO3 FMO4 FMO5 Nitric oxide synthase NOS1 NOS2 NOS3 Cholesterol 7 alpha-hydroxylase Methane monooxygenase 3A4 14α-demethylase 24-hydroxycholesterol 7α-hydroxylase
1.14.14: reduced flavin or flavoprotein	19A1 2D6 2E1
1.14.15: reduced iron–sulfur protein	11B1 11B2 11A1
1.14.16: reduced pteridine (BH4 dependent)	Phenylalanine hydroxylase Tyrosine hydroxylase Tryptophan hydroxylase
1.14.17: reduced ascorbate	Dopamine beta-hydroxylase
1.14.18-19: other	Tyrosinase Stearoyl-CoA desaturase-1
1.14.99 - miscellaneous	Cyclooxygenase Heme oxygenase (HMOX1) Squalene monooxygenase 17A1 21A2 Ecdysone 20-monooxygenase Deoxyhypusine monooxygenase

v t e 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)

Monooxygenase DBH-like 1

Deficiency

See also

References

Further reading