EC number:1.3.5.4
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.3 Acting on the CH-CH group of donors |
| 1.3.5 With a quinone or related compound as acceptor |
| ID: | 1.3.5.4 |
|---|---|
| Description: | Fumarate reductase (quinol). |
| Alternative Name: |
Succinate dehydrogenase (menaquinone). Fumarate reductase (menaquinone). |
| Cath: | 1.10.1060.10; 1.10.1130.10; 1.10.472.70; 1.20.1300.10; 1.20.5.540; 1.20.58.100; 4.10.80.40; 3.50.50.60; 3.90.700.10; 3.10.20.30; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.3.5.4 |
| BRENDA Enzyme Link: | BRENDA 1.3.5.4 |
| KEGG Enzyme Link: | KEGG1.3.5.4 |
| BioCyc Enzyme Link: | BioCyc 1.3.5.4 |
| ExPASy Enzyme Link: | ExPASy1.3.5.4 |
| EC2PDB Enzyme Link: | EC2PDB 1.3.5.4 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.3.5.4 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.3.5.4 |
| IntEnz Enzyme Link: | IntEnz 1.3.5.4 |
| MEDLINE Enzyme Link: | MEDLINE 1.3.5.4 |
| RHEA:40523 | a quinone + succinate = a quinol + fumarate |
| RULE(radius=1) | [*:1]-[C;H0;+0:2]1=[C;H0;+0:3](-[*:4])-[C;H0;+0:5](=[O;H0;+0:6])-[C;H0;+0:7](-[*:8])=[C;H0;+0:9](-[*:10])-[C;H0;+0:11]-1=[O;H0;+0:12].[*:13]-[CH2;+0:14]-[CH2;+0:15]-[*:16]>>[*:13]-[CH;+0:14]=[CH;+0:15]-[*:16].[*:1]-[c;H0;+0:2]1:[c;H0;+0:11](-[OH;+0:12]):[c;H0;+0:9](-[*:10]):[c;H0;+0:7](-[*:8]):[c;H0;+0:5](-[OH;+0:6]):[c;H0;+0:3]:1-[*:4] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| One-step purification from Escherichia coli of complex II (succinate: ubiquinone oxidoreductase) associated with succinate-reducible cytochrome b556. | Kita K, Vibat CR, Meinhardt S, Guest JR, Gennis RB | 1989 Feb 15 | 2644269 |
| Function and structure of complex II of the respiratory chain. | Cecchini G | 2003 | 14527321 |
| The four subunits of mitochondrial respiratory complex II are encoded by multiple nuclear genes and targeted to mitochondria in Arabidopsis thaliana. | Figueroa P, Léon G, Elorza A, Holuigue L, Araya A, Jordana X | 2002 Nov | 12374303 |
| RHEA:27834 | a menaquinone + succinate = a menaquinol + fumarate |
| RULE(radius=1) | [*:1]-[C;H0;+0:2]1=[C;H0;+0:3](-[*:4])-[C;H0;+0:5](=[O;H0;+0:6])-[*:7](:[cH;+0:8]:[*:9]):[c;H0;+0:10](:[*:11])-[C;H0;+0:12]-1=[O;H0;+0:13].[*:14]-[CH2;+0:15]-[CH2;+0:16]-[*:17]>>[*:14]-[CH;+0:15]=[CH;+0:16]-[*:17].[*:1]-[c;H0;+0:2]1:[c;H0;+0:3](-[*:4]):[c;H0;+0:5](-[OH;+0:6]):[*:7](:[cH;+0:10]:[*:11]):[c;H0;+0:8](:[*:9]):[c;H0;+0:12]:1-[OH;+0:13] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site. | Iverson TM, Luna-Chavez C, Croal LR, Cecchini G, Rees DC | 2002 May 3 | 11850430 |
| Structure of the Escherichia coli fumarate reductase respiratory complex. | Iverson TM, Luna-Chavez C, Cecchini G, Rees DC | 1999 Jun 18 | 10373108 |