J. Biochem, 1997, Vol. 121, No. 4 798-803
© 1997 Japanese Biochemical Society
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Structural and Functional Characterization of the Human Brain D-Aspartate Oxidase1
Department of Biochemistry, Kumamoto University School of Medicine 2–2–1 Honjo, Kumamoto 860
2To whom correspondence should be addressed. Phone: +81-96-373-5062, Fax: +81-96-373-5066 E-mail: miura{at}gpo.kumamoto-u.ac.JP
D-Aspartate oxidase (DDO) cDNAs were isolated from the human brain RNA using the RT-PCR method. Two forms (DDO-1 and DDO-2) of DDO mRNA were detected. Structural analysis of the DDO cDNAs and genomic DNA showed that DDO-1 and DDO-2 are produced by alternative splicing from a single gene. A protein encoded by the DDO-1 cDNA consists of 341 ami no acids, and the amino acid sequence of DDO-2 was identical to that of DDO-1 except for the absence of 59 amino acids covering residues 95–163 of DDO-1. A homogenous preparation of DDO-1 was obtained using an expression system in Escherichia coli. DDO-1 selectively catalyzed the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate; the values of Km and kcat for D-aspartate were 2.7 mMand 52.5 mol D-aspartate oxidized.s-1.mol-1 and those for N-methyl D-aspartate were 6.8 mM and 37.7 mol N-methyl D-aspartate oxidized.s-1.mol-1, respectively.
1This study was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science, Sports and Culture of Japan and by a Research Grant from the Japan Society for the Promotion of Science (Research for the Future). The nucleotide sequence data reported in this paper will appear in the DDBJ, EMBL, and GenBank nucleotide sequence databases with the accession number D89858 [GenBank] .
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