Monooxygenase DBH-like 1

Last updated
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
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 Mb Chr 10: 24.1 – 24.18 Mb
PubMed search [3] [4]
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]

Contents

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]

See also

Related Research Articles

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References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000079931 - Ensembl, May 2017
  2. 1 2 3 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. 1 2 3 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. PMID   11028916. S2CID   12738480.
  8. 1 2 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. 1 2 3 4 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