EC Number   |
Reaction |
Reference |
|---|
   3.11.1.1 | phosphonoacetaldehyde + H2O = acetaldehyde + phosphate |
active site structure |
650251 |
| 3.11.1.1 | phosphonoacetaldehyde + H2O = acetaldehyde + phosphate |
alternative catalytic mechanism, involving proton transfer that triggers P-C bond cleavage, transition states, TSd1, TSm1, TSd2, TSm2, and theoretical QM/MM study using crystal structure of an inhibitor-bound enzyme, overview. The bond breaking process is facilitated by proton transfer from catalytic lysine residue to the substrate. The common catalytic mechanism involves formation of a Schiff base, overview |
697292 |
| 3.11.1.1 | phosphonoacetaldehyde + H2O = acetaldehyde + phosphate |
bicovalent catalytic mechanism in which an active site nucleophile abstracts the phosphoryl group from the Schiff-base intermediate formed from Lys53 and phosphonoacetaldehyde |
246536 |
| 3.11.1.1 | phosphonoacetaldehyde + H2O = acetaldehyde + phosphate |
double displacement mechanism proceeding via protonated Schiff base and phosphoenzyme intermediates. The mechanism involves P-C bond cleavage in a protonated Schiff base intermediate by in-line displacement by an enzyme nucleophile. Subsequent hydrolysis of the resultant acetaldehyde enamine and phosphoenzyme groups then yield acetaldehyde and phosphate |
246532 |
| 3.11.1.1 | phosphonoacetaldehyde + H2O = acetaldehyde + phosphate |
imine formation between the enzyme and its substrate |
246530 |
| 3.11.1.1 | phosphonoacetaldehyde + H2O = acetaldehyde + phosphate |
mechanism involves Schiff base formation with Lys53 followed by phosphoryl transfer to Asp11 and at last hydrolysis at the imine and acyl phosphate phosphorus |
246534 |
| 3.11.1.1 | phosphonoacetaldehyde + H2O = acetaldehyde + phosphate |
mechanism involves Schiff base formation with Lys53 followed by phosphoryl transfer to Asp12 and at last hydrolysis at the imine and acyl phosphate phosphorus |
246534 |
| 3.11.1.1 | phosphonoacetaldehyde + H2O = acetaldehyde + phosphate |
mechanism, active site conformation during catalysis, Lys53 is involved |
650117 |
| 3.11.1.1 | phosphonoacetaldehyde + H2O = acetaldehyde + phosphate |
mechanism, reaction pathway, Schiff base formation between an amine and a ketone in aqueous solution, active site model |
652569 |
| 3.11.1.1 | phosphonoacetaldehyde + H2O = acetaldehyde + phosphate |
quantum chemical study of the imine formation reaction, which precedes P-C bond cleavage. The barrier of this reaction can be significantly lowered if the reaction is assisted by a water molecule and the substrate is protonated |
683906 |
