PMID: 2888479Jun 16, 1987

Molecular cloning and sequence analysis of cDNAs encoding porcine kidney D-amino acid oxidase

K FukuiY Miyake


Complementary DNAs encoding D-amino acid oxidase (EC, DAO), one of the principal and characteristic enzymes of the peroxisomes of porcine kidney, have been isolated from the porcine kidney cDNA library by hybridization with synthetic oligonucleotide probes corresponding to the partial amino acid sequences. Analysis of the nucleotide sequences of two clones revealed a complete 3211-nucleotide sequence with a 5'-terminal untranslated region of 198 nucleotides, 1041 nucleotides of an open reading frame that encoded 347 amino acids, and a 3'-terminal untranslated region of 1972 nucleotides. The deduced amino acid sequence was completely identical with the reported sequence of the mature enzyme [Ronchi, S., Minchiotti, L., Galliano, M., Curti, B., Swenson, R. P., Williams, C. H. J., & Massey, V. (1982) J. Biol. Chem. 257, 8824-8834]. These results indicate that the primary translation product does not contain a signal peptide at its amino-terminal region for its translocation into peroxisomes. RNA blot hybridization analysis suggests that porcine kidney D-amino acid oxidase is encoded by three mRNAs that differ in size: 3.3, 2.7, and 1.5 kilobases. Comparison of the sequences of the two cDNA clones revealed that multiple pol...Continue Reading


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Related Concepts

D-Amino Acid Dehydrogenase
Untranslated Regions
Enzymes, antithrombotic
DAO gene
Nucleic Acid Hybridization Procedure
Amino Acids, I.V. solution additive
Oligonucleotide Probes
Sense Codon
Sequence Analysis

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