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PMID: 2792366 Published · ppublish English Comparative Study Journal Article

Sequence similarity between dopamine beta-hydroxylase and peptide alpha-amidating enzyme: evidence for a conserved catalytic domain.

FEBS letters ·Vol. 255 ·No. 1 ·1989-09-11 ·Pages 116-20

Southan C, Kruse LI

Abstract

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.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Binding Sites Catalysis Cattle Copper/analysis Dopamine beta-Hydroxylase/analysis Humans Mixed Function Oxygenases Molecular Sequence Data Multienzyme Complexes Oxidoreductases Acting on CH-NH Group Donors/analysis Peptides/analysis Software Xenopus
Chemicals
Multienzyme Complexes Peptides Copper Mixed Function Oxygenases Dopamine beta-Hydroxylase peptidylglycine monooxygenase Oxidoreductases Acting on CH-NH Group Donors
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Southan C
Department of Medicinal Chemistry, Smith Kline & French Research Limited, Welwyn, England.
Kruse L I
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1989-09-11
Pages
116-20
Language
English
Region
England
NLM ID
0155157
Subset
IM
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