Structural interpretation of the binding of 9-azidoacridine to D-amino acid oxidase.
D-Amino acid oxidase (EC 1.4.3.3) forms an inhibited complex with the nucleotide- and aromatic-binding-site affinity reagent 9-azido[3H]acridine. Tryptic digestion of the photolysed complex yielded two radioactive peptides, 222-265 (T23) and 298-328 (T29), which core and secondary structure analysis revealed to be exposed, but which also comprised the propargylglycine-binding residues. This suggests that at least parts of the peptides containing these residues are in the active centre and that they are spatially close to the flavin-binding site.
Nicholson
B H
BH
Department of Physiology and Biochemistry, University of Reading, U.K.
Batra
S P
SP
D000595:Amino Acid Sequence; D000818:Animals; D001386:Azides / Q000494:pharmacology*; D001665:Binding Sites; D003605:D-Amino-Acid Oxidase / Q000037:antagonists & inhibitors*; D007668:Kidney / Q000201:enzymology; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000032:analysis; D010449:Peptide Mapping; D013552:Swine
D001386:Azides; D009842:Oligopeptides; C036356:9-azidoacridine; D003605:D-Amino-Acid Oxidase