Premium
Sequence similarity between dopamine β‐hydroxylase and peptide α‐amidating enzyme: Evidence for a conserved catalytic domain
Author(s) -
Southan Christopher,
Kruse Lawrence I.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81072-5
Subject(s) - monooxygenase , enzyme , structural similarity , biochemistry , homology (biology) , dopamine , peptide sequence , peptide , biology , chemistry , sequence (biology) , stereochemistry , amino acid , endocrinology , gene , cytochrome p450
A comparison of human dopamine β‐hydroxylase (EC 1.14.17.1) with bovine peptide C‐terminal α‐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.