Structural features of human monoamine oxidase A elucidated from cDNA and peptide sequences.
Monoamine oxidase (MAO), an important enzyme for the degradation of amine neurotransmitters, has been implicated in neuropsychiatric 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.
Molecular Neurogenetics Division, E. K. Shriver Center, Waltham, MA 02254.
Y P
YP
Hsu
W
W
Weyler
S
S
Chen
K B
KB
Sims
W B
WB
Rinehart
M C
MC
Utterback
J F
JF
Powell
X O
XO
Breakefield
D000244:Adenosine Diphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D004247:DNA / Q000235:genetics*; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism; D006801:Humans; D008099:Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D008995:Monoamine Oxidase / Q000235:genetics*; D010446:Peptide Fragments; D010920:Placenta / Q000201:enzymology; D012689:Sequence Homology, Nucleic Acid
D010446:Peptide Fragments; D005182:Flavin-Adenine Dinucleotide; D000244:Adenosine Diphosphate; D004247:DNA; D008995:Monoamine Oxidase