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1: Biochem J. 1988 Nov 1;255(3):907-12.Click here to read Links

Structural interpretation of the binding of 9-azidoacridine to D-amino acid oxidase.

Nicholson BH, Batra SP.

Department of Physiology and Biochemistry, University of Reading, U.K.

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.

PMID: 2905598 [PubMed - indexed for MEDLINE]

PMCID: PMC1135327