Monooxygenase DBH-like 1

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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]

Deficiency

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

References

↑ "Entrez Gene: monooxygenase, DBH-like 1".
↑ ^2.0 ^2.1 ^2.2 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.
↑ 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.
↑ ^4.0 ^4.1 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.
↑ ^5.0 ^5.1 ^5.2 ^5.3 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: 144–9. ISSN 0959-9851. PMID 12102462.

Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
Xin X, Mains RE, Eipper BA (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.
Bon S, Lamouroux A, Vigny A, Massoulié J, Mallet J, Henry JP (October 1991). "Amphiphilic and nonamphiphilic forms of bovine and human dopamine beta-hydroxylase". J. Neurochem. 57 (4): 1100–11. doi:10.1111/j.1471-4159.1991.tb08267.x. ISSN 0022-3042. PMID 1654385.

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[entrez-1] "Entrez Gene: monooxygenase, DBH-like 1".

[pmid9751809-2] 2.0 ^2.1 ^2.2 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.

[pmid11028916-3] 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 1420-682X. PMID 11028916.

[pmid2792366-4] 4.0 ^4.1 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.

[pmid15337741-5] 5.0 ^5.1 ^5.2 ^5.3 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.

[pmid12102462-6] Vincent S, Robertson D (May 2002). "The broader view: catecholamine abnormalities". Clin Auton Res. Suppl. 1: 144–9. ISSN 0959-9851. PMID 12102462.

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v t e Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)
1.14.11: 2-oxoglutarate	Prolyl hydroxylase Lysyl hydroxylase
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 Lanosterol 14 alpha-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

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme 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)

Monooxygenase DBH-like 1

Contents

Deficiency

See also

References

Further reading

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