CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.1000 | HAD superfamily/HAD-like |
Domain Context
CATH Clusters
| Superfamily | HAD superfamily/HAD-like |
| Functional Family | Enolase-phosphatase E1 |
Enzyme Information
| 3.1.3.77 |
Acireductone synthase.
based on mapping to UniProt Q9UHY7
5-(methylthio)-2,3-dioxopentyl phosphate + H(2)O = 1,2-dihydroxy-5- (methylthio)pent-1-en-3-one + phosphate.
-!- This bifunctional enzyme first enolizes the substrate to form the intermediate 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate, which is then dephosphorylated to form the acireductone 1,2- dihydroxy-5-(methylsulfanyl)pent-1-en-3-one. -!- The acireductone represents a branch point in the methione salvage pathway as it is used in the formation of formate, CO and 3-(methylsulfanyl)propanoate by EC 1.13.11.53 and of formate and 4-(methylsulfanyl)-2-oxobutanoate either by a spontaneous reaction under aerobic conditions or by EC 1.13.11.54.
|
UniProtKB Entries (1)
| Q9UHY7 |
ENOPH_HUMAN
Homo sapiens
Enolase-phosphatase E1
|
PDB Structure
| PDB | 1ZS9 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal Structure of Human E1 Enzyme and its Complex with a Substrate Analog Reveals the Mechanism of its Phosphatase/Enolase
J.Mol.Biol.
|
