| ID: | 4.2.1.129 |
|---|---|
| Description: | Squalene--hopanol cyclase. |
| Alternative Name: |
Squalene--hopene cyclase. |
| Cath: | 1.50.10.20; |
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 4.2.1.129 |
| BRENDA Enzyme Link: | BRENDA 4.2.1.129 |
| KEGG Enzyme Link: | KEGG4.2.1.129 |
| BioCyc Enzyme Link: | BioCyc 4.2.1.129 |
| ExPASy Enzyme Link: | ExPASy4.2.1.129 |
| EC2PDB Enzyme Link: | EC2PDB 4.2.1.129 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.2.1.129 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.2.1.129 |
| IntEnz Enzyme Link: | IntEnz 4.2.1.129 |
| MEDLINE Enzyme Link: | MEDLINE 4.2.1.129 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:16561 | H2O + squalene = hopan-22-ol |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](-[*:3]-[*:4]-[CH;+0:5]=[C;H0;+0:6](-[*:7])-[*:8]-[*:9]-[CH;+0:10]=[C;H0;+0:11](-[*:12])-[*:13])=[CH;+0:14]-[*:15]-[*:16]-[CH;+0:17]=[C;H0;+0:18](-[*:19])-[*:20]-[*:21]-[CH;+0:22]=[C;H0;+0:23](-[*:24])-[*:25]-[*:26]-[CH;+0:27]=[C;H0;+0:28](-[*:29])-[*:30].[OH2;+0:31]>>[*:1]-[C;H0;+0:2]12-[*:3]-[*:4]-[CH;+0:5]3-[C;H0;+0:6](-[*:7])(-[*:8]-[*:9]-[CH2;+0:10]-[C;H0;+0:11]-3(-[*:12])-[*:13])-[CH;+0:14]-1-[*:15]-[*:16]-[CH;+0:17]1-[C;H0;+0:18]-2(-[*:19])-[*:20]-[*:21]-[CH;+0:22]2-[CH;+0:27](-[C;H0;+0:28](-[*:29])(-[*:30])-[OH;+0:31])-[*:26]-[*:25]-[C;H0;+0:23]-1-2-[*:24] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Squalene-hopene cyclases. | Siedenburg G, Jendrossek D | 2011 Jun | 21531832 |
| Squalene-hopene cyclase: final deprotonation reaction, conformational analysis for the cyclization of (3R,S)-2,3-oxidosqualene and further evidence for the requirement of an isopropylidene moiety both for initiation of the polycyclization cascade and for the formation of the 5-membered E-ring. | Hoshino T, Nakano S, Kondo T, Sato T, Miyoshi A | 2004 May 21 | 15136801 |
| Site-directed mutagenesis experiments on the putative deprotonation site of squalene-hopene cyclase from Alicyclobacillus acidocaldarius. | Sato T, Kouda M, Hoshino T | 2004 Mar | 15056909 |