EC number:4.1.2.12
| ID: | 4.1.2.12 |
|---|---|
| Description: | 2-dehydropantoate aldolase. |
| Alternative Name: |
Ketopantoaldolase. 2-dehydropantoate formaldehyde-lyase. |
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 4.1.2.12 |
| BRENDA Enzyme Link: | BRENDA 4.1.2.12 |
| KEGG Enzyme Link: | KEGG4.1.2.12 |
| BioCyc Enzyme Link: | BioCyc 4.1.2.12 |
| ExPASy Enzyme Link: | ExPASy4.1.2.12 |
| EC2PDB Enzyme Link: | EC2PDB 4.1.2.12 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.1.2.12 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.1.2.12 |
| IntEnz Enzyme Link: | IntEnz 4.1.2.12 |
| MEDLINE Enzyme Link: | MEDLINE 4.1.2.12 |
| RHEA:23276 | 2-dehydropantoate = 3-methyl-2-oxobutanoate + formaldehyde |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](-[*:3])(-[*:4])-[CH2;+0:5]-[OH;+0:6]>>[*:1]-[CH;+0:2](-[*:3])-[*:4].[CH2;+0:5]=[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 |
|---|---|---|---|
| Ketopantoate formation by a hydroxy-methylation enzyme from Escherichia coli. | McINTOSH EN, PURKO M, WOOD WA | 1957 Sep | 13475336 |