Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on Enzyme Commission mapping
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
Properties of the flavoenzyme D-aspartate oxidase from Octopus vulgaris.
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DDO is a 37 kDa FAD-dependent monomer with KM 4.3 mM for D-Asp and 9.7 mM for D-Glu. Two active-site residues with pKa 7.1 and 9.1 are critical for catalysis.
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The enzyme exists in active (FAD-bound) and inactive (6-OH-FAD-bound) forms; the inactive form is a purification artifact.
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Structural similarities to bovine D-aspartate oxidase and porcine D-amino acid oxidase in amino-acid composition and N-terminal sequence.
Biological role of D-amino acid oxidase and D-aspartate oxidase. Effects of D-amino acids.
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D-amino acids administered to animals are oxidized in vivo by D-amino acid oxidase and D-aspartate oxidase in tissues, producing NH3, H2O2, and the corresponding keto acid.
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Inverse relationship between oxidase levels and D-amino acid concentrations: younger animals have lower oxidase and higher D-amino acids.
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Biological role is detoxification of D-amino acids that accumulate during aging.
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DDO expression in liver and kidney increases progressively during postnatal development.
Further study on the specificity of D-amino acid oxidase and D-aspartate oxidase and time course for complete oxidation of D-amino acids.
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D-AspO from Octopus and beef kidney specifically oxidizes D-Asp, D-Glu, D-Asn, D-Gln, D-Asp-dimethyl-ester, and N-methyl-D-Asp.
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D-Pro, D-Leu, D-Ala, D-Met oxidized at very low rates (0.2-0.6% of D-Asp rate).
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All L-amino acids are not oxidized, confirming strict D-stereoselectivity.
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D-AspO is clearly distinct from D-amino acid oxidase (D-AAO) in substrate specificity.
Occurrence of free D-aspartic acid in the circumsoesophageal ganglia of Aplysia fasciata.
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Free D-Asp found at high concentrations in CNS of cephalopods (O. vulgaris, L. vulgaris, S. officinalis) and Aplysia, constituting 8.3% of total aspartate in ganglia.
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D-Asp may have a specific neurological function in molluscan CNS.
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Octopus D-AspO was used as analytical tool to measure D-Asp levels.
Control of GnRH expression in the olfactory lobe of Octopus vulgaris.
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NMDA receptors are present in Octopus olfactory lobes and NMDA enhances GnRH mRNA expression in a dose-response manner.
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L-glutamate/NMDA/NO pathway controls reproductive maturation in O. vulgaris.
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D-aspartate acts as NMDA receptor agonist, implicating DDO in neuromodulation through regulation of D-Asp levels.
Cephalopod vision involves dicarboxylic amino acids - D-aspartate, L-aspartate and L-glutamate.
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High concentrations of free D-aspartate in cephalopod retina: O. vulgaris 2.30 +/- 0.25 umol/g, S. officinalis 2.60 +/- 0.30 umol/g, L. vulgaris 1.60 +/- 0.20 umol/g tissue.
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Purified octopus D-AspO degrades D-Asp in retinal extracts, abolishing the D-Asp HPLC peak, confirming enzyme activity against the retinal D-Asp pool.
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Radiotracer experiments indicate D-Asp is synthesized in optic lobes and transported to the retina, establishing dynamic D-Asp handling in cephalopod visual circuitry.
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DDO also oxidizes NMDA (N-methyl-D-aspartate), in addition to D-Asp and D-Glu.
Human D-aspartate oxidase - a key player in D-aspartate metabolism.
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DDO/DASPO is a peroxisomal enzyme in mammals; D-Asp and DDO are localized in neurons within peroxisomes, emphasizing compartmentalization and H2O2 handling.
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DDO inhibition could raise endogenous D-Asp to modulate NMDA-receptor-related physiology as a potential therapeutic strategy for neuropsychiatric disorders.
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Human DASPO operates by a ternary-complex mechanism where oxygen reacts with the reduced flavin-imino acid complex before product release, with hydride transfer from substrate alpha-carbon to flavin N5.