CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.970 | Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains |
Domain Context
CATH Clusters
| Superfamily | 3.40.50.970 |
| Functional Family | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase |
Enzyme Information
| 2.2.1.9 |
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase.
based on mapping to UniProt P17109
Isochorismate + 2-oxoglutarate = 5-enolpyruvoyl-6-hydroxy-2-succinyl- cyclohex-3-ene-1-carboxylate + CO(2).
-!- Involved in the biosynthesis of vitamin K(2) (menaquinone). -!- In most anaerobes and all Gram-positive aerobes, menaquinone is the sole electron transporter in the respiratory chain and is essential for their survival. -!- It had previously been thought that the products of the reaction were (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate (SHCHC), pyruvate and CO(2) but it is now known that two separate enzymes are involved: this enzyme and EC 4.2.99.20. -!- Under basic conditions, the product can spontaneously lose pyruvate to form SHCHC. -!- Formerly EC 2.5.1.64 and EC 2.5.1.n1.
|
UniProtKB Entries (1)
| P17109 |
MEND_ECOLI
Escherichia coli K-12
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
|
PDB Structure
| PDB | 5Z2U |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Two active site arginines are critical determinants of substrate binding and catalysis in MenD: a thiamine-dependent enzyme in menaquinone biosynthesis.
Biochem. J.
|