| EC Tree |
| 2. Transferases |
| 2.1 Transferring one-carbon groups |
| 2.1.2 Hydroxymethyl-, formyl- and related transferases |
| ID: | 2.1.2.11 |
|---|---|
| Description: | 3-methyl-2-oxobutanoate hydroxymethyltransferase. |
| Alternative Name: |
Ketopantoate hydroxymethyltransferase. Dehydropantoate hydroxymethyltransferase. Alpha-ketoisovalerate hydroxymethyltransferase. |
| Cath: | 3.20.20.60; |
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 2.1.2.11 |
| BRENDA Enzyme Link: | BRENDA 2.1.2.11 |
| KEGG Enzyme Link: | KEGG2.1.2.11 |
| BioCyc Enzyme Link: | BioCyc 2.1.2.11 |
| ExPASy Enzyme Link: | ExPASy2.1.2.11 |
| EC2PDB Enzyme Link: | EC2PDB 2.1.2.11 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.1.2.11 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.1.2.11 |
| IntEnz Enzyme Link: | IntEnz 2.1.2.11 |
| MEDLINE Enzyme Link: | MEDLINE 2.1.2.11 |
| RHEA:11824 | (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[*:4].[*:5]-[N;H0;+0:6]1-[*:7]-[*:8]-[N;H0;+0:9](-[*:10])-[CH2;+0:11]-1.[OH2;+0:12]>>[*:1]-[C;H0;+0:2](-[*:3])(-[*:4])-[CH2;+0:11]-[OH;+0:12].[*:5]-[NH;+0:6]-[*:7]-[*:8]-[NH;+0:9]-[*:10] |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Cloning and sequencing of the Escherichia coli panB gene, which encodes ketopantoate hydroxymethyltransferase, and overexpression of the enzyme. | Jones CE, Brook JM, Buck D, Abell C, Smith AG | 1993 Apr | 8096212 |
| Structure of E. coli ketopantoate hydroxymethyl transferase complexed with ketopantoate and Mg2+, solved by locating 160 selenomethionine sites. | von Delft F, Inoue T, Saldanha SA, Ottenhof HH, Schmitzberger F, Birch LM, Dhanaraj V, Witty M, Smith AG, Blundell TL, Abell C | 2003 Aug | 12906829 |
| Comparative analysis of the Escherichia coli ketopantoate hydroxymethyltransferase crystal structure confirms that it is a member of the (betaalpha)8 phosphoenolpyruvate/pyruvate superfamily. | Schmitzberger F, Smith AG, Abell C, Blundell TL | 2003 Jul | 12837791 |