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Structural Features of Human Monoamine Oxidase A Elucidated from cDNA and Peptide Sequences
Author(s) -
Hsu YunPung P.,
Weyler Walter,
Chen Shiuan,
Sims Katherine B.,
Rinehart William B.,
Utterback Margot C.,
Powell John F.,
Breakefield Xandra O.
Publication year - 1988
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1988.tb03105.x
Subject(s) - biochemistry , monoamine oxidase , complementary dna , flavin adenine dinucleotide , cofactor , peptide , peptide sequence , flavoprotein , flavin group , enzyme , monoamine oxidase b , monoamine oxidase a , biology , amino acid , chemistry , microbiology and biotechnology , gene
Monoamine oxidase (MAO), an important enzyme for the degradation of amine neurotransmitters, has been implicated in neu‐ropsychiatric illness. The amino acid sequence for one form of the enzyme, MAO‐A, has been deduced from human cDNA clones and verified against proteolytic peptides. The covalent binding site for the flavin adenine dinucleotide (FAD) cofactor is near the C‐terminal region. The presence of features characteristic of the ADP‐binding fold suggests that the N‐terminal region is also involved in the binding of FAD. These cDNAs should facilitate the study of the structure, function, and intracellular targeting of MAO, as well as the analysis of its expression in normal and pathological states.