EC number:1.8.99.5
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.8 Acting on a sulfur group of donors |
| 1.8.99 With unknown physiological acceptors |
| ID: | 1.8.99.5 |
|---|---|
| Description: | Dissimilatory sulfite reductase. |
| Alternative Name: |
Siroheme sulfite reductase. |
| Cath: | 1.10.10.370; 1.10.287.3170; 3.30.1420.10; 3.30.413.10; 3.30.70.20; 3.30.70.250; 3.30.70.2500; 3.30.70.3340; 3.40.50.80; 3.90.480.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.8.99.5 |
| BRENDA Enzyme Link: | BRENDA 1.8.99.5 |
| KEGG Enzyme Link: | KEGG1.8.99.5 |
| BioCyc Enzyme Link: | BioCyc 1.8.99.5 |
| ExPASy Enzyme Link: | ExPASy1.8.99.5 |
| EC2PDB Enzyme Link: | EC2PDB 1.8.99.5 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.8.99.5 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.8.99.5 |
| IntEnz Enzyme Link: | IntEnz 1.8.99.5 |
| MEDLINE Enzyme Link: | MEDLINE 1.8.99.5 |
| RHEA:47020 | [DsrC protein]-S-sulfanyl-L-cysteine/L-cysteine + 3 A + 3 H2O = [DsrC protein]-disulfide + 3 AH2 + 2 H(+) + sulfite |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[SH;+0:3].[*:4]-[SH;+0:5].[OH2;+0:6].[OH2;+0:7].[OH2;+0:8]>>[*:1]-[CH2;+0:2]-[S;H0;+0:5]-[*:4].[O;H0;+0:8]=[S;H0;+0:3](-[OH;+0:6])-[OH;+0:7] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur. | Pott AS, Dahl C | 1998 Jul | 9695921 |
| Siroheme as an active catalyst in sulfite reduction. | Seki Y, Sogawa N, Ishimoto M | 1981 Nov | 7338517 |
| The "bacterial heterodisulfide" DsrC is a key protein in dissimilatory sulfur metabolism. | Venceslau SS, Stockdreher Y, Dahl C, Pereira IA | 2014 Jul | 24662917 |
| The crystal structure of Desulfovibrio vulgaris dissimilatory sulfite reductase bound to DsrC provides novel insights into the mechanism of sulfate respiration. | Oliveira TF, Vonrhein C, Matias PM, Venceslau SS, Pereira IA, Archer M | 2008 Dec 5 | 18829451 |
| RHEA:47008 | [DsrC protein]-disulfide + 2 A + 3 H2O + hydrogen sulfide = [DsrC protein]-dithiol + 2 AH2 + H(+) + sulfite |
| RULE(radius=1) | [*:1]-[S;H0;+0:2]-[S;H0;+0:3]-[*:4].[OH2;+0:5].[OH2;+0:6].[OH2;+0:7].[SH2;+0:8]>>[*:4]-[SH;+0:3].[*:1]-[SH;+0:2].[O;H0;+0:7]=[S;H0;+0:8](-[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 |
|---|---|---|---|
| Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus. | Parey K, Warkentin E, Kroneck PM, Ermler U | 2010 Oct 19 | 20822098 |
| Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur. | Pott AS, Dahl C | 1998 Jul | 9695921 |
| Desulfoviridin, a multimeric-dissimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough). Purification, characterization, kinetics and EPR studies. | Wolfe BM, Lui SM, Cowan JA | 1994 Jul 1 | 8033912 |
| Dissimilatory sulphite reductase from Archaeoglobus fulgidus: physico-chemical properties of the enzyme and cloning, sequencing and analysis of the reductase genes. | Dahl C, Kredich NM, Deutzmann R, Trüper HG | 1993 Aug | 7691984 |
| Siroheme as an active catalyst in sulfite reduction. | Seki Y, Sogawa N, Ishimoto M | 1981 Nov | 7338517 |
| Isolation of assimilatroy- and dissimilatory-type sulfite reductases from Desulfovibrio vulgaris. | Lee JP, LeGall J, Peck HD Jr | 1973 Aug | 4725615 |
| The "bacterial heterodisulfide" DsrC is a key protein in dissimilatory sulfur metabolism. | Venceslau SS, Stockdreher Y, Dahl C, Pereira IA | 2014 Jul | 24662917 |
| The crystal structure of Desulfovibrio vulgaris dissimilatory sulfite reductase bound to DsrC provides novel insights into the mechanism of sulfate respiration. | Oliveira TF, Vonrhein C, Matias PM, Venceslau SS, Pereira IA, Archer M | 2008 Dec 5 | 18829451 |