EC number:4.1.2.17
| ID: | 4.1.2.17 |
|---|---|
| Description: | L-fuculose-phosphate aldolase. |
| Alternative Name: |
L-fuculose-1-phosphate lactaldehyde-lyase. L-fuculose 1-phosphate aldolase. Fuculose aldolase. |
| Cath: | 1.20.1250.20; 3.40.225.10; |
3D structure
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.References
External Links
| UniProtKB Enzyme Link: | UniProtKB 4.1.2.17 |
| BRENDA Enzyme Link: | BRENDA 4.1.2.17 |
| KEGG Enzyme Link: | KEGG4.1.2.17 |
| BioCyc Enzyme Link: | BioCyc 4.1.2.17 |
| ExPASy Enzyme Link: | ExPASy4.1.2.17 |
| EC2PDB Enzyme Link: | EC2PDB 4.1.2.17 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.1.2.17 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.1.2.17 |
| IntEnz Enzyme Link: | IntEnz 4.1.2.17 |
| MEDLINE Enzyme Link: | MEDLINE 4.1.2.17 |
| RHEA:12933 | L-fuculose 1-phosphate = (S)-lactaldehyde + dihydroxyacetone phosphate |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[CH;+0:4](-[*:5])-[OH;+0:6]>>[*:1]-[CH2;+0:2]-[*:3].[*:5]-[CH;+0:4]=[O;H0;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure. | Dreyer MK, Schulz GE | 1996 Jun 14 | 8676381 |
| Structures of l-fuculose-1-phosphate aldolase mutants outlining motions during catalysis. | Joerger AC, Mueller-Dieckmann C, Schulz GE | 2000 Nov 3 | 11054289 |
| Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis. | Joerger AC, Gosse C, Fessner WD, Schulz GE | 2000 May 23 | 10821675 |