Monooxygenase DBH-like 1

Monooxygenase DBH-like 1
Monooxygenase, DBH-like 1
Identifiers
Symbols MOXD1; DKFZp564G202; MOX; PRO5780; dJ248E1.1
External IDs OMIM: 609000 MGI: 1921582 HomoloGene: 22904 GeneCards: MOXD1 Gene
EC number 1.14.17.1
RNA expression pattern
PBB GE MOXD1 26002 at tn.png
More reference expression data
Protein domains
Q6UVY6 HUMAN ProteinDomains SMART.png
Orthologs
Species Human Mouse
Entrez 26002 59012
Ensembl ENSG00000079931 ENSMUSG00000020000
UniProt Q6UVY6 Q9CXI3
RefSeq (mRNA) NM_015529 NM_021509.5
RefSeq (protein) NP_056344 NP_067484.2
Location (UCSC) Chr 6:
132.62 – 132.72 Mb		 Chr 10:
23.94 – 24.02 Mb
PubMed search [1] [2]

DBH-like monooxygenase protein 1, also known as monooxygenase X, is an enzyme that in humans is encoded by the MOXD1 gene.[1][2]

DBH-like 1 maintains many of the structural features of dopamine beta-monooxygenase DBH.[3] Since Peptidylglycine alpha-hydroxylating monooxygenase (PHM; EC 1.14.17.3) is homologous to dopamine beta-monooxygenase (DBM; EC 1.14.17.1)[4] this concerns a structural basis for a new family of copper type II, significantly specific for ascorbate-dependent monooxygenases[4] based on the corresponding mouse homolog.[2] The pathway of catecholamine synthesis is a possible catecholamine-binding metabolic copper[5] enzyme domain, a neuron-like property encoding MOX without a signal sequence enzyme metabolism resolving the monooxygenase X chemical pathway[5] of an unknown substrate,[2] exogenous MOX is not secreted, and it localizes throughout the endoplasmic reticulum,[5] in both endocrine or nonendocrine cells.[5]

Contents

Deficiency

DBH deficiency has been treated effectively with L-threo-3,4-dihydroxyphenylserine (DOPS).[6]

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. ^ "Entrez Gene: monooxygenase, DBH-like 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26002. 
  2. ^ 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". Gene 218 (1-2): 111–20. doi:10.1016/S0378-1119(98)00344-8. PMID 9751809. 
  3. ^ 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 1420682X. PMID 11028916. 
  4. ^ 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. 
  5. ^ 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. 
  6. ^ Vincent S, Robertson D. (May 2002). "The broader view: catecholamine abnormalities.". Clin Auton Res. Suppl. 1: 144–9. ISSN 0959-9851. PMID 12102462. 

Further reading


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