Sequence similarity between dopamine beta-hydroxylase and peptide alpha-amidating enzyme: evidence for a conserved catalytic domain.
A comparison of human dopamine beta-hydroxylase (EC 1.14.17.1) with bovine peptide C-terminal alpha-amidating enzyme (EC 1.14.17.3), revealed a 28% identity extending throughout a common catalytic domain of approximately 270 residues. The shared biochemical properties of these two enzymes from neurosecretory granules suggests that the sequence similarity reflects a genuine homology and provides a structural basis for a new family of copper type II, ascorbate-dependent monooxygenases.
Southan
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Department of Medicinal Chemistry, Smith Kline & French Research Limited, Welwyn, England.
Kruse
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D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D002384:Catalysis; D002417:Cattle; D003300:Copper / Q000032:analysis; D004299:Dopamine beta-Hydroxylase / Q000032:analysis*; D006801:Humans; D006899:Mixed Function Oxygenases; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000032:analysis*; D010455:Peptides / Q000032:analysis; D012984:Software; D014981:Xenopus
D009097:Multienzyme Complexes; D010455:Peptides; D003300:Copper; D006899:Mixed Function Oxygenases; D004299:Dopamine beta-Hydroxylase; C035189:peptidylglycine monooxygenase; D000587:Oxidoreductases Acting on CH-NH Group Donors