Dopamine beta-hydroxylase (DBH; EC 1.14.17.1 ), the enzyme that converts dopamine to norepinephrine, is present in
the synaptic vesicles of postganglionic sympathetic neurons. Release of norepinephrine is accompanied by the
simultaneous release of DBH.
NCBI 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.
General function
Enzyme, Oxidoreductase
Comment
Cellular localization
Cytoplasmic
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Ovarian function
Steroid metabolism
Comment
Kotwica J, et al reported that dopamine-beta-hydroxylase inhibitor, inhibited
the stimulating effect of dopamine on luteal progesterone and OT content.
Expression regulated by
Comment
Ovarian localization
Oocyte, Luteal cells
Comment
Mayerhofer A, reported that intraovarian neurons contain tyrosine hydroxylase (TH), the
rate-limiting enzyme in catecholamine biosynthesis. They showed that the primate ovary expresses both the
genes encoding TH and dopamine beta-hydroxylase (DBH), the key enzymes in
norepinephrine (NE) biosynthesis. Ovarian neurons were identified as a site of
TH and DBH gene expression, and oocytes were identified as an
exclusive site of DBH synthesis.
Battista PJ et al demonstrate the
existence of DA and NE in bovine luteal tissue and indicate that exogenous DA
can be converted to NE in luteal tissue. The results support a physiological role
for catecholamines in the stimulation of bovine luteal function.