DBH-like 1 maintains many of the structural features of dopamine beta-monooxygenaseDBH.[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]
^ abSouthan 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. PMID2792366. S2CID84464131.
