The primary structure of the flavoprotein D-aspartate oxidase from beef kidney.
The complete primary structure of the peroxisomal flavoenzyme D-aspartate oxidase from beef kidney has been determined by analyses of the peptides obtained through fragmentation of the carboxymethylated protein with trypsin, CNBr, heptafluorobutyric acid/CNBr and Staphylococcus aureus V8 protease. The protein consists of a single polypeptide of 338 residues, accounting for a M(r) of 37,305 for the apoprotein. A form of the enzyme lacking Lys-338 and therefore ending with Pro-337 has been detected. The N-terminal residue is blocked. Seven cysteines and no disulfide bridges are present. Residue 228 can be either Ile or Val. Thus, D-aspartate oxidase presents two types of heterogeneity in the polypeptide chain in addition to the one already described concerning the possible content of FAD or 6-hydroxyflavin adenine dinucleotide. Comparison of the primary structure of D-aspartate oxidase with other known sequences reveals that D-aspartate oxidase is homologous with D-amino acid oxidase (another flavo-oxidase) and does not present significant sequence similarities with any other protein, including flavoenzymes.
Negri
A
A
Instituto di Fisiologia Veterinaria e Biochimica, Università di Milano, Italy.
Ceciliani
F
F
Tedeschi
G
G
Simonic
T
T
Ronchi
S
S
D000594:Amino Acid Oxidoreductases / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003488:Cyanogen Bromide; D050804:D-Aspartate Oxidase; D005182:Flavin-Adenine Dinucleotide / Q000032:analysis; D005466:Fluorocarbons; D007668:Kidney / Q000201:enzymology*; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D012697:Serine Endopeptidases; D014357:Trypsin
D005466:Fluorocarbons; D005182:Flavin-Adenine Dinucleotide; C033094:perfluorobutyric acid; D000594:Amino Acid Oxidoreductases; D050804:D-Aspartate Oxidase; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D014357:Trypsin; D003488:Cyanogen Bromide