Dopamine beta-hydroxylase

GWB-74AC41

Specific for the ~75k DBH protein in Western blots of human adrenal medulla. Also recognizes DBH in monkey tissues.

3 4-dihydroxyphenethylamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O. Cofactor: Binds 1 PQQ per subunit. Cofactor: Binds 2 copper ions per subunit.

Homotetramer.

Activity is enhanced by nerve growth factor (in superior cervical ganglia and adrenal medulla). Trans-synaptic stimulation with reserpine acetylcholine and glucocorticoids.

Defects in DBH are the cause of DBH deficiency [MIM:223360]; also called norepinephrine deficiency or noradrenaline deficiency. This disorder is characterized by profound deficits in autonomic and cardiovascular function but apparently only subtle signs if any of central nervous system dysfunction.

Contains 1 DOMON domain. Summary: The protein encoded by this gene is an oxidoreductase belonging to the copper type II ascorbate-dependent monooxygenase family. It is present in the synaptic vesicles of postganglionic sympathetic neurons and converts dopamine to norepinephrine. It exists in both soluble and membrane-bound forms depending on the absence or presence respectively of a signal peptide. [1] Tang Y. Anderson G. M. Zabetian C. P. Kohnke M. D. and Cubells J. F. et al. Haplotype-controlled analysis of the association of a non-synonymous single nucleotide polymorphism at DBH (+ 1603C --& gt; T) with plasma dopamine beta-hydroxylase activity[2] Abe M. Wu Z. Yamamoto M. Jin J. J. Tabara Y. Mogi M. Kohara K. Miki T. and Nakura J. Association of dopamine beta-hydroxylase polymorphism with hypertension through interaction with fasting plasma glucose in Japanese[3] Depondt C. Cock H. R. Healy D. G. Burley M. W. Weinshenker D. Wood N. W. Goldstein D. B. and Sisodiya S. M. The -1021C-& gt; T DBH gene variant is not associated with epilepsy or antiepileptic drug response[4] Inkster B. Muglia P. Jain U. and Kennedy J. L. et al. Linkage disequilibrium analysis of the dopamine beta-hydroxylase gene in persistent attention deficit hyperactivity disorder[5] Anderson N. L. Polanski M. Pieper R. Gatlin T. Tirumalai R. S. Conrads T. P. Veenstra T. D. Adkins J. N. Pounds J. G. Fagan R. and et al. The human plasma proteome: a nonredundant list developed by combination of four separate sources[6] Kobayashi K. Kurosawa Y. Fukita K. Nagatsu T. Human dopamine beta-hydroxylase gene: two mRNA types having different 3\' -terminal regions are produced through alternative polyadenylation. [7] Lamouroux A. Vigny A. Faucon Biguet N. Darmon M. C. Franck R. Henry J. -P. Mallet J. The primary structure of human dopamine-beta-hydroxylase: insights into the relationship between the soluble and the membrane-bound forms of the enzyme. [8] Humphray S. J. Oliver K. Hunt A. R. Plumb R. W. Loveland J. E. Howe K. L. Andrews T. D. Searle S. Hunt S. E. Scott C. E. et al. DNA sequence and analysis of human chromosome 9. [9] Strausberg R. L. Feingold E. A. Grouse L. H. Derge J. G. Klausner R. D. Collins F. S. Wagner L. Shenmen C. M. Schuler G. D. Altschul S. F. et al. Generation and initial analysis of more than 15 000 full-length human and mouse cDNA sequences. [10] Li B. Tsing S. Kosaka A. H. Nguyen B. Osen E. G. Bach C. Chan H. Barnett J. Expression of human dopamine beta-hydroxylase in Drosophila Schneider 2 cells.