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Literature summary extracted from
- D-amino acid oxidase: physiological role and applications (2008), Biochemistry (Moscow), 73, 1511-1518.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 1.4.3.3 | analysis | the enzyme is useful as a model FAD-containing protein | Sus scrofa |
| 1.4.3.3 | medicine | the purified recombinant or native enzyme is used in therapeutic treatment of cancer combined with injection of D-proline. The enzyme is a target in the development of medical treatment for neurodegeneration and cancer | Homo sapiens |
| 1.4.3.3 | synthesis | pig kidney enzyme is used to make L-pipecolic acid from a racemic mixture via D-isomer oxidation | Sus scrofa |
| 1.4.3.3 | synthesis | the enzyme is used to develop biocatalysts for the production of 7-aminocephalosporanic acid from the natural antibiotic cephalosporin C, and to produce optically active L-methionine from D-amino acid with the yield of 100% in a cascade system of four enzymes, or to produce phenyl pyruvate from D-phenylalanine with the yield of 99% | Trigonopsis variabilis |
| 1.4.3.3 | synthesis | the enzyme is used to produce phenyl pyruvate from D-phenylalanine with the yield of 99% | Rhodotorula toruloides |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.4.3.3 | recombinant enzyme expression in Escherichia coli | Homo sapiens |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.4.3.3 | crystallization of a single point mutant, X-ray diffraction structure determination and analysis at 1.8 A resolution | Trigonopsis variabilis |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.4.3.3 | additional information | construction of point mutants with altered substrate specificity compared to the wild-type enzyme, the created mutant forms of TvDAAO are perfectly suitable for selective determination of D-Ser in excess of D-Ala, D-Asp, and D-Pro | Trigonopsis variabilis |
| 1.4.3.3 | additional information | for development of a micro-biosensor for determination of D-serine in vivo, the enzyme is adsorbed on a cylindrical platinum microelectrode covered by a layer of poly-m-phenylenediamine, a selective mediator for H2O2 | Sus scrofa |
| 1.4.3.3 | additional information | for development of a micro-biosensor for determination of D-serine in vivo, the enzyme is physically adsorbed on an electrode surface. For in vivo experiments, the enzyme layer is protected with an additional Nafion membrane | Rhodotorula toruloides |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.4.3.3 | D-3,4-dihydroxyphenylalanine + H2O + O2 | Homo sapiens | - |
? + H2O2 + NH3 | - |
? |  |
| 1.4.3.3 | D-alanine + H2O + O2 | Trigonopsis variabilis | - |
pyruvate + NH3 + H2O2 | - |
? | |
| 1.4.3.3 | D-alanine + H2O + O2 | Homo sapiens | - |
pyruvate + H2O2 + NH3 | - |
? | |
| 1.4.3.3 | D-proline + H2O + O2 | Trigonopsis variabilis | - |
2-oxopentanoate + NH3 + H2O2 | - |
? | |
| 1.4.3.3 | D-serine + H2O + O2 | Homo sapiens | - |
2-oxo-3-hydroxypropionate + NH3 + H2O2 | - |
? | |
| 1.4.3.3 | D-serine + H2O + O2 | Trigonopsis variabilis | - |
2-oxo-3-hydroxypropionate + NH3 + H2O2 | - |
? | |
| 1.4.3.3 | additional information | Homo sapiens | the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview | ? | - |
? | |
| 1.4.3.3 | additional information | Sus scrofa | the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview | ? | - |
? | |
| 1.4.3.3 | additional information | Trigonopsis variabilis | the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview | ? | - |
? | |
| 1.4.3.3 | additional information | Rhodotorula toruloides | the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.4.3.3 | Homo sapiens | - |
- |
- |
| 1.4.3.3 | Rhodotorula toruloides | P80324 | - |
- |
| 1.4.3.3 | Sus scrofa | - |
- |
- |
| 1.4.3.3 | Trigonopsis variabilis | Q99042 | - |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.4.3.3 | kidney | - |
Homo sapiens | - |
| 1.4.3.3 | kidney | - |
Sus scrofa | - |
| 1.4.3.3 | liver | - |
Homo sapiens | - |
| 1.4.3.3 | liver | - |
Sus scrofa | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.4.3.3 | D-3,4-dihydroxyphenylalanine + H2O + O2 | - |
Homo sapiens | ? + H2O2 + NH3 | - |
? | |
| 1.4.3.3 | D-3,4-dihydroxyphenylalanine + H2O + O2 | best substrate | Homo sapiens | ? + H2O2 + NH3 | - |
? | |
| 1.4.3.3 | D-alanine + H2O + O2 | - |
Trigonopsis variabilis | pyruvate + NH3 + H2O2 | - |
? | |
| 1.4.3.3 | D-alanine + H2O + O2 | - |
Homo sapiens | pyruvate + H2O2 + NH3 | - |
? | |
| 1.4.3.3 | D-proline + H2O + O2 | - |
Trigonopsis variabilis | 2-oxopentanoate + NH3 + H2O2 | - |
? | |
| 1.4.3.3 | D-serine + H2O + O2 | - |
Homo sapiens | 2-oxo-3-hydroxypropionate + NH3 + H2O2 | - |
? | |
| 1.4.3.3 | D-serine + H2O + O2 | - |
Trigonopsis variabilis | 2-oxo-3-hydroxypropionate + NH3 + H2O2 | - |
? | |
| 1.4.3.3 | additional information | the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview | Homo sapiens | ? | - |
? | |
| 1.4.3.3 | additional information | the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview | Sus scrofa | ? | - |
? | |
| 1.4.3.3 | additional information | the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview | Trigonopsis variabilis | ? | - |
? | |
| 1.4.3.3 | additional information | the mechanism of the enzyme regulation is complex and multi-parametric because the same enzyme simultaneously influences the level of different D-amino acids, which can result in opposing effects, overview | Rhodotorula toruloides | ? | - |
? | |
| 1.4.3.3 | additional information | the enzyme catalyzes oxidative deamination of D-amino acids yielding hydrogen peroxide and an imino acid. The latter is further non-enzymatically hydrolyzed to an alpha-keto acid and ammonium. DAAO is highly specific towards D-isomers of amino acids, it is almost inactive towards the corresponding L-isomer | Homo sapiens | ? | - |
? | |
| 1.4.3.3 | additional information | the enzyme catalyzes oxidative deamination of D-amino acids yielding hydrogen peroxide and an imino acid. The latter is further non-enzymatically hydrolyzed to an alpha-keto acid and ammonium. DAAO is highly specific towards D-isomers of amino acids, it is almost inactive towards the corresponding L-isomer | Sus scrofa | ? | - |
? | |
| 1.4.3.3 | additional information | the enzyme catalyzes oxidative deamination of D-amino acids yielding hydrogen peroxide and an imino acid. The latter is further non-enzymatically hydrolyzed to an alpha-keto acid and ammonium. DAAO is highly specific towards D-isomers of amino acids, it is almost inactive towards the corresponding L-isomer | Rhodotorula toruloides | ? | - |
? | |
| 1.4.3.3 | additional information | the enzyme catalyzes oxidative deamination of D-amino acids yielding hydrogen peroxide and an imino acid. The latter is further non-enzymatically hydrolyzed to an alpha-keto acid and ammonium. DAAO is highly specific towards D-isomers of amino acids, it is almost inactive towards the corresponding L-isomer. The wild-type enzyme is inactive towards D-Asp, being however very active with D-Ala | Trigonopsis variabilis | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.4.3.3 | DAAO | - |
Homo sapiens |
| 1.4.3.3 | DAAO | - |
Sus scrofa |
| 1.4.3.3 | DAAO | - |
Trigonopsis variabilis |
| 1.4.3.3 | DAAO | - |
Rhodotorula toruloides |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.4.3.3 | FAD | dependent on | Homo sapiens | |
| 1.4.3.3 | FAD | dependent on | Sus scrofa | |
| 1.4.3.3 | FAD | dependent on | Trigonopsis variabilis | |
| 1.4.3.3 | FAD | dependent on | Rhodotorula toruloides | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.4.3.3 | physiological function | physiological role of D-amino acids and DAAOs, regulation of the nervous system, hormone secretion, and other processes by D-amino acids, detailed overview | Homo sapiens |
| 1.4.3.3 | physiological function | physiological role of D-amino acids and DAAOs, regulation of the nervous system, hormone secretion, and other processes by D-amino acids, detailed overview | Sus scrofa |
| 1.4.3.3 | physiological function | physiological role of D-amino acids and DAAOs, regulation of the nervous system, hormone secretion, and other processes by D-amino acids, detailed overview | Trigonopsis variabilis |
| 1.4.3.3 | physiological function | physiological role of D-amino acids and DAAOs, regulation of the nervous system, hormone secretion, and other processes by D-amino acids, detailed overview | Rhodotorula toruloides |
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