EC number:2.5.1.21
Enzyme
Download| EC Tree |
| 2. Transferases |
| 2.5 Transferring alkyl or aryl groups, other than methyl groups |
| 2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date) |
3D structure
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References
External Links
| UniProtKB Enzyme Link: | UniProtKB 2.5.1.21 |
| BRENDA Enzyme Link: | BRENDA 2.5.1.21 |
| KEGG Enzyme Link: | KEGG2.5.1.21 |
| BioCyc Enzyme Link: | BioCyc 2.5.1.21 |
| ExPASy Enzyme Link: | ExPASy2.5.1.21 |
| EC2PDB Enzyme Link: | EC2PDB 2.5.1.21 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.5.1.21 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.5.1.21 |
| IntEnz Enzyme Link: | IntEnz 2.5.1.21 |
| MEDLINE Enzyme Link: | MEDLINE 2.5.1.21 |
| RHEA:32299 | 2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate + NAD(+) + squalene |
| RULE(radius=1) | [*:1]-[N;H0;+0:2]1-[CH;+0:3]=[C;H0;+0:4](-[*:5])-[CH2;+0:6]-[CH;+0:7]=[CH;+0:8]-1.[*:9]-[O;H0;+0:10]-[CH2;+0:11]-[*:12].[*:13]-[O;H0;+0:14]-[CH2;+0:15]-[*:16].[H+;H0:17]>>[*:12]-[CH2;+0:11]-[CH2;+0:15]-[*:16].[*:9]-[OH;+0:10].[*:13]-[OH;+0:14].[*:1]-[n+;H0:2]1:[cH;+0:3]:[c;H0;+0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1 |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Recombinant squalene synthase. A mechanism for the rearrangement of presqualene diphosphate to squalene. | Blagg BS, Jarstfer MB, Rogers DH, Poulter CD | 2002 Jul 31 | 12137537 |
| Structure and regulation of mammalian squalene synthase. | Tansey TR, Shechter I | 2000 Dec 15 | 11111077 |
| Crystal structure of human squalene synthase. A key enzyme in cholesterol biosynthesis. | Pandit J, Danley DE, Schulte GK, Mazzalupo S, Pauly TA, Hayward CM, Hamanaka ES, Thompson JF, Harwood HJ Jr | 2000 Sep 29 | 10896663 |
| Squalene synthase: steady-state, pre-steady-state, and isotope-trapping studies. | Radisky ES, Poulter CD | 2000 Feb 22 | 10677224 |
| RHEA:32295 | 2 (2E,6E)-farnesyl diphosphate + H(+) + NADPH = 2 diphosphate + NADP(+) + squalene |
| RULE(radius=1) | [*:1]-[N;H0;+0:2]1-[CH;+0:3]=[C;H0;+0:4](-[*:5])-[CH2;+0:6]-[CH;+0:7]=[CH;+0:8]-1.[*:9]-[O;H0;+0:10]-[CH2;+0:11]-[*:12].[*:13]-[O;H0;+0:14]-[CH2;+0:15]-[*:16].[H+;H0:17]>>[*:12]-[CH2;+0:11]-[CH2;+0:15]-[*:16].[*:9]-[OH;+0:10].[*:13]-[OH;+0:14].[*:1]-[n+;H0:2]1:[cH;+0:3]:[c;H0;+0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1 |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Recombinant squalene synthase. A mechanism for the rearrangement of presqualene diphosphate to squalene. | Blagg BS, Jarstfer MB, Rogers DH, Poulter CD | 2002 Jul 31 | 12137537 |
| Structure and regulation of mammalian squalene synthase. | Tansey TR, Shechter I | 2000 Dec 15 | 11111077 |
| Crystal structure of human squalene synthase. A key enzyme in cholesterol biosynthesis. | Pandit J, Danley DE, Schulte GK, Mazzalupo S, Pauly TA, Hayward CM, Hamanaka ES, Thompson JF, Harwood HJ Jr | 2000 Sep 29 | 10896663 |
| Squalene synthase: steady-state, pre-steady-state, and isotope-trapping studies. | Radisky ES, Poulter CD | 2000 Feb 22 | 10677224 |