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evolution
DBH is a member of a small unique class of copper-containing hydroxylases that are found in eukaryotes, and all play a critical role in the biosynthesis of neurotransmitters and hormones. The other members of the family are the bifunctional enzyme peptidylglycine alpha-hydroxylating (and alpha-amidating) monooxygenase (PHM), monooxygenase X (DBH-like monooxygenase protein 1, MOXD1), and tyramine beta-monooxygease (TBH), which is the insect homologue of DBH
evolution
the enzyme belongs to the copper type II, ascorbate-dependent monooxygenases
evolution
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the enzyme belongs to the copper type II, ascorbate-dependent monooxygenases
malfunction
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dopamine-beta-hydroxylase knockout mice are more sensitive to stress but survive a single 2 h restraint stress in a tube. Disruption of the DBH gene blocks the stress-induced elevation of tyrosine hydroxylase mRNA levels in adrenal medulla but increases phenylethanolamine N-methyltransferase gene expression in both adrenal medulla and stellate ganglia
malfunction
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in the GRDBHCre mice, glucocorticoid receptor (GR) immunoreactivity is lost in chromaffin cells but is unaltered in the cortex, which leads to the loss of the A-synthesizing enzyme phenylethanolamine-N-methyl-transferase (PNMT). GRDBHCre mutants are viable and fertile and do not appear different from control littermates. Degeneration of the adrenal medulla in young GRDBHCre mutants
malfunction
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no major role of the -1021C>T polymorphism or the gene itself in the development of cocaine addiction in a Brazilian sample of 689 cocaine addicts and 832 healthy controls, even after correction for sex age, education and population stratification
malfunction
enzyme activity and norepinephrine level in shrimps downregulated by LvDBH-dsRNA are reduced, the treated animals show increased susceptibility to Vibrio alginolyticus infection, significantly lower total hemocyte count, phagocytic activity, clearance efficiency, and resistance to Vibrio alginolyticus infection are observed in shrimp that received LvDBH-dsRNA at 3 days post injection compared to those injected with diethyl pyrocarbonate-water or non-targeting gene-dsRNA
malfunction
enzyme LvDBH inhibited or silenced in haemocytes by disulfiram and LvDBH-dsRNA, repectively, results in impaired synthesis of norepinephrine from dopamine in hemolymph
malfunction
genotype-phenotype correlations. Mutant L317P shows secretory deficiency and is localized in the endoplasmic reticulum
physiological function
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DBH promoter contains at least one functional Egr1 motif, Egr1 may play a role in the physiological regulation of transcription of the DBH gene
physiological function
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determinant role of Phox2a and Phox2b on the expression and function of DBH in vitro
physiological function
Drosophila sp. (in: flies)
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tyramine beta-monooxygenase is homologous to mammalian dopamine beta-monooxygenase, tighter regulation of neurotransmitter levels by the insect enzyme than in the mammalian homologue
physiological function
dopamine beta-hydroxylase (DBH) catalyzes the conversion of dopamine to norepinephrine in the biosynthesis of catecholamines. The enzyme plays a critical role in catecholamine synthesis of neuroendocrine regulatory network, and is suggested to be involved in the immunoendocrine responses of invertebrate against bacterial challenge
physiological function
dopamine beta-hydroxylase (DBH) is a copper-containing monooxygenase enzyme that plays an important role in catecholamine synthesis of the neuroendocrine regulatory network. In shrimp, the biosynthesis of catecholamines, including dopamine and norepinephrine, is required for physiological and immunological responses against stress
physiological function
dopamine beta-hydroxylase (DBH) is the enzyme catalyzing the synthesis of noradrenaline from dopamine, it is stronger in the glomus cells of spontaneously hypertensive SHR/Izm rats than in those of Wistar Kyoto WKY/Izm rats
physiological function
dopamine beta-hydroxylase catalyzes the conversion of dopamine to norepinephrine in the biosynthesis of catecholamines
physiological function
dopamine beta-hydroxylase catalyzes the conversion of dopamine to norepinephrine in the biosynthesis of catecholamines. Effect of wild-type and mutant alpha-SYN on cAMP response element (CRE)-mediated regulation of the norepinephrine-synthesizing enzyme dopamine beta-hydroxylase (DBH): overexpression of wild-type or mutant human alpha-SYN interfers with CRE-mediated regulation of DBH transcription in norepinephrine-producing SK-N-BE(2) cells. Upon entering the nucleus, alpha-SYN interacts with the DBH promoter region encompassing the CRE, which interfered with forskolin-induced CREB binding to the CRE region. Mutant A53T alpha-SYN shows much higher tendency to nuclear translocation and interaction with the DBH promoter region encompassing the CRE than wild-type. CRE-mediated transcriptional regulation of tyrosine hydroxylase and enzyme DBH plays a crucial role in stress response
physiological function
dopamine beta-hydroxylase catalyzes the conversion of dopamine to norepinephrine in the biosynthesis of catecholamines. Effect of wild-type and mutant human alpha-SYN on cAMP response element (CRE)-mediated regulation of the norepinephrine-synthesizing enzyme dopamine beta-hydroxylase (DBH), stress-induced DBH regulation is modulated in the brains of A53T transgenic mice (A53T Tg). Overexpression of wild-type or mutant human alpha-SYN interfers with CRE-mediated regulation of DBH transcription in murine brains of A53T transgenic mice (A53T Tg). Upon entering the nucleus, alpha-SYN interacts with the DBH promoter region encompassing the CRE, which interfers with forskolin-induced CREB binding to the CRE region. Mutant A53T alpha-SYN shows much higher tendency to nuclear translocation and interaction with the DBH promoter region encompassing the CRE than wild-type
physiological function
dopamine beta-hydroxylase is a critical enzyme in the biosynthesis of catecholamines with a role in neuroendocrine regulation and in avian reproduction. Dopamine beta-hydroxylase catalyzes the conversion of dopamine to norepinephrine in the biosynthesis of catecholamines. The activity of DBH influences the levels of dopamine and the biosynthesis of norepinephrine and epinephrine. The enzyme is important in the nervous system
physiological function
dopamine-beta-hydroxylase (DBH) is an oxidoreductase that is primarily responsible for the conversion of dopamine to norepinephrine. DBH is widely regarded as a disease-modifying gene in psychiatric diseases
physiological function
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dopamine beta-hydroxylase (DBH) is the enzyme catalyzing the synthesis of noradrenaline from dopamine, it is stronger in the glomus cells of spontaneously hypertensive SHR/Izm rats than in those of Wistar Kyoto WKY/Izm rats
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additional information
enzyme structure-function relationship, overview
additional information
enzyme structure analysis, detailed overview