Compact archived record and sequence evidence for A0A7E6FSU6
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.