EC number:1.4.3.3
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.4 Acting on the CH-NH2 group of donors |
| 1.4.3 With oxygen as acceptor |
| ID: | 1.4.3.3 | ||
|---|---|---|---|
| Description: | D-amino-acid oxidase. | ||
| Prosite: | PDOC00573; | ||
| PDB: |
|
||
| Cath: | 3.30.9.10; 3.40.50.720; 3.50.50.60; |
3D structure
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.References
External Links
| UniProtKB Enzyme Link: | UniProtKB 1.4.3.3 |
| BRENDA Enzyme Link: | BRENDA 1.4.3.3 |
| KEGG Enzyme Link: | KEGG1.4.3.3 |
| BioCyc Enzyme Link: | BioCyc 1.4.3.3 |
| ExPASy Enzyme Link: | ExPASy1.4.3.3 |
| EC2PDB Enzyme Link: | EC2PDB 1.4.3.3 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.4.3.3 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.4.3.3 |
| IntEnz Enzyme Link: | IntEnz 1.4.3.3 |
| MEDLINE Enzyme Link: | MEDLINE 1.4.3.3 |
| RHEA:37583 | D-lysine + H2O + O2 = 6-amino-2-oxohexanoate + H2O2 + NH4(+) |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[NH2;+0:4].[O;H0;+0:5]=[O;H0;+0:6].[OH2;+0:7]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:7].[NH3;+0:4].[OH;+0:5]-[OH;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Identification of the initial steps in D-lysine catabolism in Pseudomonas putida. | Revelles O, Wittich RM, Ramos JL | 2007 Apr | 17259313 |
| RHEA:21816 | a D-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+) |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[NH2;+0:4].[O;H0;+0:5]=[O;H0;+0:6].[OH2;+0:7]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:7].[NH3;+0:4].[OH;+0:5]-[OH;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Identification of the histidine residue in D-amino acid oxidase that is covalently modified during inactivation by 5-dimethylaminonaphthalene-1-sulfonyl chloride. | Swenson RP, Williams CH Jr, Massey V | 1983 Jan 10 | 6129252 |
| Chemical modification of D-amino acid oxidase. Amino acid sequence of the tryptic peptides containing tyrosine and lysine residues modified by fluorodinitrobenzene. | Swenson RP, Williams CH Jr, Massey V | 1982 Feb 25 | 6120171 |
| Crystal structure of human D-amino acid oxidase: context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring. | Kawazoe T, Tsuge H, Pilone MS, Fukui K | 2006 Dec | 17088322 |
| Studies on Phe-228 and Leu-307 recombinant mutants of porcine kidney D-amino acid oxidase: expression, purification, and characterization. | Miyano M, Fukui K, Watanabe F, Takahashi S, Tada M, Kanashiro M, Miyake Y | 1991 Jan | 1673125 |
| D-AMINO ACID OXIDASE. 3. EFFECT OF PH. | DIXON M, KLEPPE K | 1965 Mar 22 | 14314379 |
| D-AMINO ACID OXIDASE. I. DISSOCIATION AND RECOMBINATION OF THE HOLOENZYME. | DIXON M, KLEPPE K | 1965 Mar 22 | 14314378 |
| The purification and some properties of D-amino acid oxidase. | MASSEY V, PALMER G, BENNETT R | 1961 Mar 18 | 13767909 |