EC number:1.6.3.2
| ID: | 1.6.3.2 |
|---|---|
| Description: | NAD(P)H oxidase (H(2)O-forming). |
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 1.6.3.2 |
| BRENDA Enzyme Link: | BRENDA 1.6.3.2 |
| KEGG Enzyme Link: | KEGG1.6.3.2 |
| BioCyc Enzyme Link: | BioCyc 1.6.3.2 |
| ExPASy Enzyme Link: | ExPASy1.6.3.2 |
| EC2PDB Enzyme Link: | EC2PDB 1.6.3.2 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.6.3.2 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.6.3.2 |
| IntEnz Enzyme Link: | IntEnz 1.6.3.2 |
| MEDLINE Enzyme Link: | MEDLINE 1.6.3.2 |
| RHEA:37799 | 2 H(+) + 2 NADH + O2 = 2 H2O + 2 NAD(+) |
| RULE(radius=1) | [*:1]-[C;H0;+0:2]1=[CH;+0:3]-[N;H0;+0:4](-[*:5])-[CH;+0:6]=[CH;+0:7]-[CH2;+0:8]-1.[*:9]-[N;H0;+0:10]1-[CH;+0:11]=[C;H0;+0:12](-[*:13])-[CH2;+0:14]-[CH;+0:15]=[CH;+0:16]-1.[H+;H0:17].[H+;H0:18].[O;H0;+0:19]=[O;H0;+0:20]>>[*:1]-[c;H0;+0:2]1:[cH;+0:3]:[n+;H0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[*:9]-[n+;H0:10]1:[cH;+0:11]:[c;H0;+0:12](-[*:13]):[cH;+0:14]:[cH;+0:15]:[cH;+0:16]:1.[OH2;+0:19].[OH2;+0:20] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| O2 and reactive oxygen species detoxification complex, composed of O2-responsive NADH:rubredoxin oxidoreductase-flavoprotein A2-desulfoferrodoxin operon enzymes, rubperoxin, and rubredoxin, in Clostridium acetobutylicum. | Kawasaki S, Sakai Y, Takahashi T, Suzuki I, Niimura Y | 2009 Feb | 19124587 |
| Molecular cloning and sequence analysis of the gene encoding the H2O-forming NADH oxidase from Streptococcus mutans. | Matsumoto J, Higuchi M, Shimada M, Yamamoto Y, Kamio Y | 1996 Jan | 8824824 |
| Identification of two distinct NADH oxidases corresponding to H2O2-forming oxidase and H2O-forming oxidase induced in Streptococcus mutans. | Higuchi M, Shimada M, Yamamoto Y, Hayashi T, Koga T, Kamio Y | 1993 Oct | 8254304 |
| Isolation and properties of an H2O-forming NADH oxidase from Streptococcus faecalis. | Schmidt HL, Stöcklein W, Danzer J, Kirch P, Limbach B | 1986 Apr 1 | 3082630 |
| Cloning and characterization of a thermostable H2O-forming NADH oxidase from Lactobacillus rhamnosus. | Zhang YW, Tiwari MK, Gao H, Dhiman SS, Jeya M, Lee JK | 2012 Apr 5 | 22418266 |
| An archaeal NADH oxidase causes damage to both proteins and nucleic acids under oxidative stress. | Jia B, Lee S, Pham BP, Cho YS, Yang JK, Byeon HS, Kim JC, Cheong GW | 2010 Apr | 20213313 |
| Reductive dioxygen scavenging by flavo-diiron proteins of Clostridium acetobutylicum. | Hillmann F, Riebe O, Fischer RJ, Mot A, Caranto JD, Kurtz DM Jr, Bahl H | 2009 Jan 5 | 19084524 |
| Hexameric ring structure of a thermophilic archaeon NADH oxidase that produces predominantly H2O. | Jia B, Park SC, Lee S, Pham BP, Yu R, Le TL, Han SW, Yang JK, Choi MS, Baumeister W, Cheong GW | 2008 Nov | 18959761 |
| Purification and characterization of an H2O-forming NADH oxidase from Clostridium aminovalericum: existence of an oxygen-detoxifying enzyme in an obligate anaerobic bacteria. | Kawasaki S, Ishikura J, Chiba D, Nishino T, Niimura Y | 2004 Apr | 15014929 |
| RHEA:37795 | 2 H(+) + 2 NADPH + O2 = 2 H2O + 2 NADP(+) |
| RULE(radius=1) | [*:1]-[C;H0;+0:2]1=[CH;+0:3]-[N;H0;+0:4](-[*:5])-[CH;+0:6]=[CH;+0:7]-[CH2;+0:8]-1.[*:9]-[N;H0;+0:10]1-[CH;+0:11]=[C;H0;+0:12](-[*:13])-[CH2;+0:14]-[CH;+0:15]=[CH;+0:16]-1.[H+;H0:17].[H+;H0:18].[O;H0;+0:19]=[O;H0;+0:20]>>[*:1]-[c;H0;+0:2]1:[cH;+0:3]:[n+;H0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[*:9]-[n+;H0:10]1:[cH;+0:11]:[c;H0;+0:12](-[*:13]):[cH;+0:14]:[cH;+0:15]:[cH;+0:16]:1.[OH2;+0:19].[OH2;+0:20] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| An archaeal NADH oxidase causes damage to both proteins and nucleic acids under oxidative stress. | Jia B, Lee S, Pham BP, Cho YS, Yang JK, Byeon HS, Kim JC, Cheong GW | 2010 Apr | 20213313 |
| Hexameric ring structure of a thermophilic archaeon NADH oxidase that produces predominantly H2O. | Jia B, Park SC, Lee S, Pham BP, Yu R, Le TL, Han SW, Yang JK, Choi MS, Baumeister W, Cheong GW | 2008 Nov | 18959761 |