Monooxygenase DBH-like 1

(Redirected from MOXD1)

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
AliasesMOXD1, MOX, PRO5780, dJ248E1.1, Monooxygenase DBH-like 1, monooxygenase DBH like 1
External IDsOMIM: 609000; MGI: 1921582; HomoloGene: 22904; GeneCards: MOXD1; OMA:MOXD1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_015529

NM_021509

RefSeq (protein)

NP_056344

NP_067484

Location (UCSC)Chr 6: 132.3 – 132.4 MbChr 10: 24.1 – 24.18 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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]

Deficiency

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DBH deficiency has been treated effectively with L-threo-3,4-dihydroxyphenylserine (DOPS).[10]

See also

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  • 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

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000079931Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020000Ensembl, 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. ^ 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.
  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. ^ 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.
  9. ^ 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.
  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

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