3.11.1.1: phosphonoacetaldehyde hydrolase
This is an abbreviated version!
For detailed information about phosphonoacetaldehyde hydrolase, go to the full flat file.
Word Map on EC 3.11.1.1
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3.11.1.1
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phosphorus
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phosphonates
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carbon-phosphorus
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dehalogenase
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phosphonoacetate
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2-aminoethylphosphonate
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schiff-base
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organophosphonate
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phosphonopyruvate
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phosphomutase
- 3.11.1.1
- phosphorus
- phosphonates
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carbon-phosphorus
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dehalogenase
- phosphonoacetate
- 2-aminoethylphosphonate
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schiff-base
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organophosphonate
- phosphonopyruvate
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phosphomutase
Reaction
Synonyms
2-phosphonoacetaldehyde phosphonohydrolase, 2-phosphonoacetylaldehyde phosphonohydrolase, hydrolase, phosphonoacetylaldehyde, P-Ald hydrolase, phosphonatase
ECTree
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Reaction
Reaction on EC 3.11.1.1 - phosphonoacetaldehyde hydrolase
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mechanism involves Schiff base formation with Lys53 followed by phosphoryl transfer to Asp11 and at last hydrolysis at the imine and acyl phosphate phosphorus
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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
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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
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phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
Schiff base formation with catalytic Lys and phosphonoacetaldehyde, PC-bond cleavage in the Schiff base takes place during the second partial reaction and liberation of the acetaldehyde from the resulting enamine occurs during the third partial reaction
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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
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phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
Schiff base mechanism
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phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
imine formation between the enzyme and its substrate
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phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
active site structure
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
mechanism, active site conformation during catalysis, Lys53 is involved
phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
mechanism, reaction pathway, Schiff base formation between an amine and a ketone in aqueous solution, active site model
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
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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
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phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
Schiff base formation with catalytic Lys and phosphonoacetaldehyde, PC-bond cleavage in the Schiff base takes place during the second partial reaction and liberation of the acetaldehyde from the resulting enamine occurs during the third partial reaction
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