| ID: | 1.16.3.3 |
|---|---|
| Description: | Manganese oxidase. |
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.| UniProtKB Enzyme Link: | UniProtKB 1.16.3.3 |
| BRENDA Enzyme Link: | BRENDA 1.16.3.3 |
| KEGG Enzyme Link: | KEGG1.16.3.3 |
| BioCyc Enzyme Link: | BioCyc 1.16.3.3 |
| ExPASy Enzyme Link: | ExPASy1.16.3.3 |
| EC2PDB Enzyme Link: | EC2PDB 1.16.3.3 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.16.3.3 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.16.3.3 |
| IntEnz Enzyme Link: | IntEnz 1.16.3.3 |
| MEDLINE Enzyme Link: | MEDLINE 1.16.3.3 |
| RHEA:52240 | 2 H2O + 2 Mn(2+) + O2 = 4 H(+) + 2 MnO2 |
| RULE(radius=1) | [Mn+2;H0:1].[Mn+2;H0:2].[O;H0;+0:3]=[O;H0;+0:4].[OH2;+0:5].[OH2;+0:6]>>[O;H0;+0:3]=[Mn;H0;+0:1]=[O;H0;+0:4].[O;H0;+0:5]=[Mn;H0;+0:2]=[O;H0;+0:6] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| CotA, a multicopper oxidase from Bacillus pumilus WH4, exhibits manganese-oxidase activity. | Su J, Bao P, Bai T, Deng L, Wu H, Liu F, He J | 2013 | 23577125 |
| Elimination of manganese(II,III) oxidation in Pseudomonas putida GB-1 by a double knockout of two putative multicopper oxidase genes. | Geszvain K, McCarthy JK, Tebo BM | 2013 Jan | 23124227 |
| A multicopper oxidase is essential for manganese oxidation and laccase-like activity in Pedomicrobium sp. ACM 3067. | Ridge JP, Lin M, Larsen EI, Fegan M, McEwan AG, Sly LI | 2007 Apr | 17359266 |
| Localization of Mn(II)-oxidizing activity and the putative multicopper oxidase, MnxG, to the exosporium of the marine Bacillus sp. strain SG-1. | Francis CA, Casciotti KL, Tebo BM | 2002 Dec | 12420165 |