Contents

Search


dopamine beta-hydroxylase (DBH)

Function: - conversion of dopamine to noradrenaline - catecholamine biosynthesis 3,4-dihydroxyphenethylamine + ascorbate + O2 noradrenaline + dehydroascorbate + H2O Cofactor: - binds 1 PQQ per subunit - binds 2 copper ions per subunit Structure: - homotetramer composed of two non-covalently bound disulfide-linked dimers - belongs to the copper type 2 ascorbate-dependent monooxygenase family - contains 1 DOMON domain Compartment: - soluble dopamine beta-hydroxylase: cytoplasmic vesicle, secretory vesicle lumen, chromaffin granule lumen - secretory vesicle membrane - chromaffin granule membrane Expression: - activity is enhanced by nerve growth factor (in superior cervical ganglia & adrenal medulla) - trans-synaptic stimulation with reserpine, acetylcholine & glucocorticoids Polymorphism: - 2 main alleles of DBH: a) DBH-A with Ala- 318 b) DBH-B with Ser-318 Pathology: - defects in DBH are the cause of dopamine-beta hydroxylase deficiency

Interactions

molecular events

General

glycoprotein hydroxylase; monooxygenase membrane protein

Properties

SIZE: entity length = 617 aa MW = 69 kD COMPARTMENT: cytoplasm cellular membrane MOTIF: transmembrane domain {17-37} Intragranular {38-617} MOTIF: DOMON {57-173} N-glycosylation site {N64} cysteine residue {C154} MODIFICATION: cysteine residue {C596} N-glycosylation site {N184} tyrosine residue {Y230} cysteine residue {C232} MODIFICATION: cysteine residue {C283} copper [Cu]-binding site SITE: 262-262 MOTIF: histidine residue (3) copper [Cu]-binding site SITE: 263-263 MOTIF: histidine residue (3) cysteine residue {C269} MODIFICATION: cysteine residue {C295} cysteine residue {C283} MODIFICATION: cysteine residue {C232} cysteine residue {C295} MODIFICATION: cysteine residue {C269} copper [Cu]-binding site SITE: 333-333 MOTIF: histidine residue (3) cysteine residue {C390} MODIFICATION: cysteine residue {C503} cysteine residue {C394} MODIFICATION: cysteine residue {C565} histidine residue {H412} copper [Cu]-binding site SITE: 412-412 MOTIF: histidine residue (3) copper [Cu]-binding site SITE: 414-414 MOTIF: histidine residue (3) cysteine residue {C466} MODIFICATION: cysteine residue {C488} copper [Cu]-binding site SITE: 487-487 MOTIF: histidine residue (3) cysteine residue {C488} MODIFICATION: cysteine residue {C466} cysteine residue {C503} MODIFICATION: cysteine residue {C390} cysteine residue {C528} MODIFICATION: cysteine residue {C-INTERCHAIN} cysteine residue {C530} MODIFICATION: cysteine residue {C-INTERCHAIN } cysteine residue {C565} MODIFICATION: cysteine residue {C394} cysteine residue {C596} MODIFICATION: cysteine residue {C154}

Database Correlations

OMIM 223360 UniProt P09172 PFAM correlations Kegg hsa:1621 ENZYME 1.14.17.1

References

  1. UniProt :accession P09172
  2. GeneReviews https://www.genecards.org/cgi-bin/carddisp.pl?gene=DBH
  3. Wikipedia, dopamine beta hydroxylase entry http://en.wikipedia.org/wiki/dopamine_beta_hydroxylase