ArticleThe Biochemical journal1997
cDNA cloning and expression of the flavoprotein D-aspartate oxidase from bovine kidney cortex.
Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 43 citations in OpenAlex.
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- Effects of a Glycosylated Form of Active Vitamin D Combined with Natural Triterpenes on Sow Productive Performance, Mineral Homeostasis, Immune Biomarkers and Serum Proteome.Veterinary sciences · 2026Article
- Relation between proteome characterization and semen quality in Italian chicken breeds.PloS one · 2025Article
- D-cysteine is an endogenous regulator of neural progenitor cell dynamics in the mammalian brain.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Review
- D-aspartate regulates melanocortin formation and function: behavioral alterations in D-aspartate oxidase-deficient mice.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
- C-terminal tripeptide Ser-Asn-Leu (SNL) of human D-aspartate oxidase is a functional peroxisome-targeting signal.The Biochemical journal · 1998Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The isolation and sequencing of the complete cDNA coding for a d-aspartate oxidase, as well as the overexpression of the recombinant active enzyme, are reported for the first time. This 2022 bp cDNA, beside the coding portion, comprises a 5' untranslated tract and the whole 3' region including the polyadenylation signal and the poly(A) tail. The encoded protein comprises 341 amino acids, with the last three residues (-Ser-Lys-Leu) representing a peroxisomal targeting signal 1 (PTS1), hitherto unknown for this protein. The overexpression of recombinant d-aspartate oxidase was achieved in a prokaryotic system, and a soluble and active enzyme was obtained which accounted for about 10% of total bacterial protein. Comparisons with the known cDNAs for mammalian d-amino acid oxidase, another peroxisomal enzyme, are also made. The close structural and functional similarities shared by these enzymes at the protein level are not reflected at the nucleic acid level.
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