EC Number   |
General Information |
Reference  |
|---|
    1.14.17.1 | malfunction |
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 |
701704 |
| 1.14.17.1 | malfunction |
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 |
701996 |
| 1.14.17.1 | physiological function |
DBH promoter contains at least one functional Egr1 motif, Egr1 may play a role in the physiological regulation of transcription of the DBH gene |
702956 |
| 1.14.17.1 | malfunction |
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 |
703462 |
| 1.14.17.1 | physiological function |
tyramine beta-monooxygenase is homologous to mammalian dopamine beta-monooxygenase, tighter regulation of neurotransmitter levels by the insect enzyme than in the mammalian homologue |
704443 |
| 1.14.17.1 | physiological function |
determinant role of Phox2a and Phox2b on the expression and function of DBH in vitro |
705254 |
| 1.14.17.1 | 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 |
-, 744191 |
| 1.14.17.1 | 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 |
744598 |
| 1.14.17.1 | 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 |
744851 |
| 1.14.17.1 | 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 |
744851 |
