Monooxygenase DBH-like 1

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

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
Gene location (Human) Chr. Chromosome 6 (human)[1] Band 6q23.2 Start 132,296,055 bp[1] End 132,401,475 bp[1]
Gene location (Mouse) Chr. Chromosome 10 (mouse)[2] Band 10|10 A4 Start 24,099,415 bp[2] End 24,178,688 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ganglionic eminence periodontal fiber gallbladder stromal cell of endometrium gastric mucosa myometrium left adrenal gland right adrenal gland smooth muscle tissue upper lobe of left lung Top expressed in vas deferens lip hair follicle molar sciatic nerve external carotid artery trigeminal ganglion skin of back internal carotid artery olfactory epithelium 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 [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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]