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Literature summary extracted from
- Properties and applications of microbial D-amino acid oxidases: current state and perspectives (2008), Appl. Microbiol. Biotechnol., 78, 1-16.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 1.4.3.3 | biotechnology | the biotechnological applications of the enzyme range from biocatalysis to convert cephalosporin C into 7-amino cephalosporanic acid to gene therapy for tumor treatment | Trigonopsis variabilis |
| 1.4.3.3 | biotechnology | the biotechnological applications of the enzyme range from biocatalysis to convert cephalosporin C into 7-amino cephalosporanic acid to gene therapy for tumor treatment | [Candida] boidinii |
| 1.4.3.3 | biotechnology | the biotechnological applications of the enzyme range from biocatalysis to convert cephalosporin C into 7-amino cephalosporanic acid to gene therapy for tumor treatment | Rubrobacter xylanophilus |
| 1.4.3.3 | biotechnology | the biotechnological applications of the enzyme range from biocatalysis to convert cephalosporin C into 7-amino cephalosporanic acid to gene therapy for tumor treatment | Mycobacterium leprae |
| 1.4.3.3 | biotechnology | the biotechnological applications of the enzyme range from biocatalysis to convert cephalosporin C into 7-amino cephalosporanic acid to gene therapy for tumor treatment | Glutamicibacter protophormiae |
| 1.4.3.3 | biotechnology | the biotechnological applications of the enzyme range from biocatalysis to convert cephalosporin C into 7-amino cephalosporanic acid to gene therapy for tumor treatment | Fusarium solani |
| 1.4.3.3 | biotechnology | the biotechnological applications of the enzyme range from biocatalysis to convert cephalosporin C into 7-amino cephalosporanic acid to gene therapy for tumor treatment | Rhodotorula toruloides |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.4.3.3 | - |
Trigonopsis variabilis |
| 1.4.3.3 | - |
[Candida] boidinii |
| 1.4.3.3 | - |
Rubrobacter xylanophilus |
| 1.4.3.3 | - |
Mycobacterium leprae |
| 1.4.3.3 | - |
Glutamicibacter protophormiae |
| 1.4.3.3 | - |
Fusarium solani |
| 1.4.3.3 | - |
Rhodotorula toruloides |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.4.3.3 | Fusarium solani | P24552 | - |
- |
| 1.4.3.3 | Glutamicibacter protophormiae | Q7X2D3 | - |
- |
| 1.4.3.3 | Mycobacterium leprae | Q9RIA4 | putative | - |
| 1.4.3.3 | Rhodotorula toruloides | P80324 | formerly Rhodotorula gracilis | - |
| 1.4.3.3 | Rubrobacter xylanophilus | Q1AYM8 | putative; strain DSM 9941 | - |
| 1.4.3.3 | Trigonopsis variabilis | Q99042 | - |
- |
| 1.4.3.3 | [Candida] boidinii | Q9HGY3 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.4.3.3 | cephalosporin C + H2O + O2 | - |
Trigonopsis variabilis | 7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2 | - |
? |  |
| 1.4.3.3 | cephalosporin C + H2O + O2 | - |
[Candida] boidinii | 7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2 | - |
? | |
| 1.4.3.3 | cephalosporin C + H2O + O2 | - |
Rubrobacter xylanophilus | 7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2 | - |
? | |
| 1.4.3.3 | cephalosporin C + H2O + O2 | - |
Mycobacterium leprae | 7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2 | - |
? | |
| 1.4.3.3 | cephalosporin C + H2O + O2 | - |
Glutamicibacter protophormiae | 7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2 | - |
? | |
| 1.4.3.3 | cephalosporin C + H2O + O2 | - |
Fusarium solani | 7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2 | - |
? | |
| 1.4.3.3 | cephalosporin C + H2O + O2 | - |
Rhodotorula toruloides | 7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2 | - |
? | |
| 1.4.3.3 | additional information | DAAOs can be divided into two groups regarding their substrate specificity, the first group prefers amino acids with small apolar side chains (D-Ala is the best substrate), the second group prefers D-amino acids possessing large hydrophobic side chains such as D-Trp, D-Met, D-Val, and D-Phe, usually the small amino acid Gly and the charged (acidic or basic) amino acids are poor DAAO substrates | Trigonopsis variabilis | ? | - |
? | |
| 1.4.3.3 | additional information | DAAOs can be divided into two groups regarding their substrate specificity, the first group prefers amino acids with small apolar side chains (D-Ala is the best substrate), the second group prefers D-amino acids possessing large hydrophobic side chains such as D-Trp, D-Met, D-Val, and D-Phe, usually the small amino acid Gly and the charged (acidic or basic) amino acids are poor DAAO substrates | [Candida] boidinii | ? | - |
? | |
| 1.4.3.3 | additional information | DAAOs can be divided into two groups regarding their substrate specificity, the first group prefers amino acids with small apolar side chains (D-Ala is the best substrate), the second group prefers D-amino acids possessing large hydrophobic side chains such as D-Trp, D-Met, D-Val, and D-Phe, usually the small amino acid Gly and the charged (acidic or basic) amino acids are poor DAAO substrates | Rubrobacter xylanophilus | ? | - |
? | |
| 1.4.3.3 | additional information | DAAOs can be divided into two groups regarding their substrate specificity, the first group prefers amino acids with small apolar side chains (D-Ala is the best substrate), the second group prefers D-amino acids possessing large hydrophobic side chains such as D-Trp, D-Met, D-Val, and D-Phe, usually the small amino acid Gly and the charged (acidic or basic) amino acids are poor DAAO substrates | Mycobacterium leprae | ? | - |
? | |
| 1.4.3.3 | additional information | DAAOs can be divided into two groups regarding their substrate specificity, the first group prefers amino acids with small apolar side chains (D-Ala is the best substrate), the second group prefers D-amino acids possessing large hydrophobic side chains such as D-Trp, D-Met, D-Val, and D-Phe, usually the small amino acid Gly and the charged (acidic or basic) amino acids are poor DAAO substrates | Glutamicibacter protophormiae | ? | - |
? | |
| 1.4.3.3 | additional information | DAAOs can be divided into two groups regarding their substrate specificity, the first group prefers amino acids with small apolar side chains (D-Ala is the best substrate), the second group prefers D-amino acids possessing large hydrophobic side chains such as D-Trp, D-Met, D-Val, and D-Phe, usually the small amino acid Gly and the charged (acidic or basic) amino acids are poor DAAO substrates | Fusarium solani | ? | - |
? | |
| 1.4.3.3 | additional information | DAAOs can be divided into two groups regarding their substrate specificity, the first group prefers amino acids with small apolar side chains (D-Ala is the best substrate), the second group prefers D-amino acids possessing large hydrophobic side chains such as D-Trp, D-Met, D-Val, and D-Phe, usually the small amino acid Gly and the charged (acidic or basic) amino acids are poor DAAO substrates | Rhodotorula toruloides | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.4.3.3 | D-amino acid oxidase | - |
Trigonopsis variabilis |
| 1.4.3.3 | D-amino acid oxidase | - |
[Candida] boidinii |
| 1.4.3.3 | D-amino acid oxidase | - |
Rubrobacter xylanophilus |
| 1.4.3.3 | D-amino acid oxidase | - |
Mycobacterium leprae |
| 1.4.3.3 | D-amino acid oxidase | - |
Glutamicibacter protophormiae |
| 1.4.3.3 | D-amino acid oxidase | - |
Fusarium solani |
| 1.4.3.3 | D-amino acid oxidase | - |
Rhodotorula toruloides |
| 1.4.3.3 | DAAO | - |
Trigonopsis variabilis |
| 1.4.3.3 | DAAO | - |
[Candida] boidinii |
| 1.4.3.3 | DAAO | - |
Rubrobacter xylanophilus |
| 1.4.3.3 | DAAO | - |
Mycobacterium leprae |
| 1.4.3.3 | DAAO | - |
Glutamicibacter protophormiae |
| 1.4.3.3 | DAAO | - |
Fusarium solani |
| 1.4.3.3 | DAAO | - |
Rhodotorula toruloides |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.4.3.3 | 30 | - |
after 30min incubation at 45°C, the activity is completely lost | Rhodotorula toruloides |
| 1.4.3.3 | 45 | - |
fully stable up to 45°C (100% of residual activity after 30 min incubation) | Trigonopsis variabilis |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.4.3.3 | 6 | 8.2 | stable from pH 6.0 to 8.2, above which a slight but continuous decrease in protein stability is observed | Trigonopsis variabilis |
| 1.4.3.3 | 6 | 8.2 | stable from pH 6.0 to 8.2, above which a slight but continuous decrease in protein stability is observed | Rubrobacter xylanophilus |
| 1.4.3.3 | 6 | 8.2 | stable from pH 6.0 to 8.2, above which a slight but continuous decrease in protein stability is observed | Mycobacterium leprae |
| 1.4.3.3 | 6 | 8.2 | stable from pH 6.0 to 8.2, above which a slight but continuous decrease in protein stability is observed | Glutamicibacter protophormiae |
| 1.4.3.3 | 6 | 8.2 | stable from pH 6.0 to 8.2, above which a slight but continuous decrease in protein stability is observed | Fusarium solani |
| 1.4.3.3 | 6 | 8.2 | stable from pH 6.0 to 8.2, above which a slight but continuous decrease in protein stability is observed | Rhodotorula toruloides |
| 1.4.3.3 | 10.5 | - |
remains fully stable up to pH 10.5 | [Candida] boidinii |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.4.3.3 | FAD | contains a molecule of noncovalently bound FAD per subunit | [Candida] boidinii | |
| 1.4.3.3 | FAD | contains one molecule of noncovalently bound FAD per subunit | Trigonopsis variabilis | |
| 1.4.3.3 | FAD | contains one molecule of noncovalently bound FAD per subunit | Rubrobacter xylanophilus | |
| 1.4.3.3 | FAD | contains one molecule of noncovalently bound FAD per subunit | Mycobacterium leprae | |
| 1.4.3.3 | FAD | contains one molecule of noncovalently bound FAD per subunit | Glutamicibacter protophormiae | |
| 1.4.3.3 | FAD | contains one molecule of noncovalently bound FAD per subunit | Fusarium solani | |
| 1.4.3.3 | FAD | contains one molecule of noncovalently bound FAD per subunit | Rhodotorula toruloides | |
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Release 2023.1 (January 2023)
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