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
mechanism involves Schiff base formation with Lys53 followed by phosphoryl transfer to Asp12 and at last hydrolysis at the imine and acyl phosphate phosphorus
mechanism involves Schiff base formation with Lys53 followed by phosphoryl transfer to Asp11 and at last hydrolysis at the imine and acyl phosphate phosphorus
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
bicovalent catalytic mechanism in which an active site nucleophile abstracts the phosphoryl group from the Schiff-base intermediate formed from Lys53 and phosphonoacetaldehyde
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
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
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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SYSTEMATIC NAME
IUBMB Comments
2-oxoethylphosphonate phosphonohydrolase
This enzyme destabilizes the C-P bond, by forming an imine between one of its lysine residues and the carbonyl group of the substrate, thus allowing this, normally stable, bond to be broken. The mechanism is similar to that used by EC 4.1.2.13, fructose-bisphosphate aldolase, to break a C-C bond. Belongs to the haloacetate dehalogenase family.
2-aminoethylphosphonic acid:pyruvate aminotransferase and phosphonoacetaldehyde hydrolase activities are induced when cells are both phosphate limited and supplied with 2-aminoethylphosphonic acid as sole source of phosphorus in the culture medium. Neither enzyme is induced in phosphate-replete medium, or in medium where both 2-aminoethylphosphoonic acid and phosphate are supplied
2-aminoethylphosphonic acid:pyruvate aminotransferase and phosphonoacetaldehyde hydrolase activities are induced when cells are both phosphate limited and supplied with 2-aminoethylphosphonic acid as sole source of phosphorus in the culture medium. Neither enzyme is induced in phosphate-replete medium, or in medium where both 2-aminoethylphosphoonic acid and phosphate are supplied
strain NG2 can utilize 2-aminoethylphosphonic acid as sole carbon and energy, nitrogen and phosphorus source. Both 2-aminoethylphosphonic acid:pyruvate aminotransferase and phosphonoacetaldehyde hydrolase activities are inducible by the presence of 2-aminoethylphosphonic acid in the culture medium
strain NG2 can utilize 2-aminoethylphosphonic acid as sole carbon and energy, nitrogen and phosphorus source. Both 2-aminoethylphosphonic acid:pyruvate aminotransferase and phosphonoacetaldehyde hydrolase activities are inducible by the presence of 2-aminoethylphosphonic acid in the culture medium
the enzyme is involved in biodegradation pathway of ciliatine or 2-aminoethylphosphonic acid, a two-step process. The first reaction reported as transamination is carried out by 2-aminoethylphosphonic acid transaminase and leads to the formation of phosphonoacetaldehyde and corresponding amino acid. The next step includes hydrolytic cleavage of the C-P bond within the phosphonoacetaldehyde molecule and results in formation of inorganic phosphate and acetaldehyde, carried out by the phosphonoacetaldehyde hydrolase. The phophonoacetaldehyde hydrolase hydrolyzes
the enzyme is involved in the phosphonatase pathway of 2-aminoethyl phosphonate degradation also including a 2-AEP:pyruvate aminotransferase (EC 2.6.1.37), encoded by gene phnW, whose products are phosphonoacetaldehyde and alanine. Phosphate-starvation-inducible expression of this pathway as a part of the Pho regulon
the enzyme is involved in the phosphonatase pathway of 2-aminoethyl phosphonate degradation also including a 2-AEP:pyruvate aminotransferase (EC 2.6.1.37), encoded by gene phnW, whose products are phosphonoacetaldehyde and alanine. Expression of the operon is substrate-inducible, mediated by the product of an adjacent gene that encodes a LysR-like transcriptional activator, LTTR
the enzyme is involved in the phosphonatase pathway of 2-aminoethyl phosphonate degradation also including a 2-AEP:pyruvate aminotransferase (EC 2.6.1.37), encoded by gene phnW, whose products are phosphonoacetaldehyde and alanine. Expression of the operon is substrate-inducible, mediated by the product of an adjacent gene that encodes a LysR-like transcriptional activator, LTTR
the enzyme is involved in the phosphonatase pathway of 2-aminoethyl phosphonate degradation also including a 2-AEP:pyruvate aminotransferase (EC 2.6.1.37), encoded by gene phnW, whose products are phosphonoacetaldehyde and alanine. Phosphate-starvation-inducible expression of this pathway as a part of the Pho regulon
the enzyme is involved in biodegradation pathway of ciliatine or 2-aminoethylphosphonic acid, a two-step process. The first reaction reported as transamination is carried out by 2-aminoethylphosphonic acid transaminase and leads to the formation of phosphonoacetaldehyde and corresponding amino acid. The next step includes hydrolytic cleavage of the C-P bond within the phosphonoacetaldehyde molecule and results in formation of inorganic phosphate and acetaldehyde, carried out by the phosphonoacetaldehyde hydrolase. The phophonoacetaldehyde hydrolase hydrolyzes
the enzyme is involved in the phosphonatase pathway of 2-aminoethyl phosphonate degradation also including a 2-AEP:pyruvate aminotransferase (EC 2.6.1.37), encoded by gene phnW, whose products are phosphonoacetaldehyde and alanine. Expression of the operon is substrate-inducible, mediated by the product of an adjacent gene that encodes a LysR-like transcriptional activator, LTTR
the mechanism of C-P bond cleavage by phosphonatase involves the formation of a Schiff base intermediate between a lysine residue at the active site of the enzyme and the phosphonoacetaldehyde carbonyl group, this activates the phosphonate group for attack by an active site nucleophile
the mechanism of C-P bond cleavage by phosphonatase involves the formation of a Schiff base intermediate between a lysine residue at the active site of the enzyme and the phosphonoacetaldehyde carbonyl group, this activates the phosphonate group for attack by an active site nucleophile
the mechanism of C-P bond cleavage by phosphonatase involves the formation of a Schiff base intermediate between a lysine residue at the active site of the enzyme and the phosphonoacetaldehyde carbonyl group, this activates the phosphonate group for attack by an active site nucleophile
the mechanism of C-P bond cleavage by phosphonatase involves the formation of a Schiff base intermediate between a lysine residue at the active site of the enzyme and the phosphonoacetaldehyde carbonyl group, this activates the phosphonate group for attack by an active site nucleophile
the mechanism of C-P bond cleavage by phosphonatase involves the formation of a Schiff base intermediate between a lysine residue at the active site of the enzyme and the phosphonoacetaldehyde carbonyl group, this activates the phosphonate group for attack by an active site nucleophile
i.e. Pald, cleavage via Schiff base intermediate formed with Lys53, bound substrate stabilizes the closed conformation of the active site, thus facilitating catalysis
catalysis within the core domain of phosphonatase requires the participation of loop 5 of the corresponding cap domain. Gly is an indispensable component
activates, required for catalysis, serves as a cofactor, binds via ligation to the loop 1 Asp12 carboxylate and Thr 14 backbone carbonyl and to the loop 4 Asp186carboxylate, the loop 4 Asp190 forms a hydrogen bond to the Mg(II) water ligand, Asp186 is essential while Asp190 simply enhances cofactor binding
both 2-aminoethylphosphonic acid:pyruvate aminotransferase and phosphonoacetaldehyde hydrolase activities are inducible by the presence of 2-aminoethylphosphonic acid in the culture medium
both 2-aminoethylphosphonic acid:pyruvate aminotransferase and phosphonoacetaldehyde hydrolase activities are inducible by the presence of 2-aminoethylphosphonic acid in the culture medium
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
10 mg/ml purified recombinant wild-type and mutant enzymes, complexed with Mg2+ only or with Mg2+ and inhibitor vinyl sulfonate, in 1 mM HEPES, 10 mM MgCl2, 0.1 mM DTT, pH 7.5, 4°C, hanging drop vapour diffusion method, equal volume of protein and reservoir solution, the latter containing 30% PEG 4000, 100 mM Tris-HCl, pH 7.4, 100 mM MgCl2, 1 week, against the reservoir well solution additionally with 20% glycerol before data collection, X-ray diffraction structure determination and analysis at 2.4-2.8 A resolution
10 mg/ml wild-type and mutant D12A enzymes complexed with Mg2+ only or with Mg2+ and substrate, in 1 mM HEPES, 10 mM MgCl2, 0.1 mM DTT, pH 7.5, 4°C, hanging drop vapour diffusion method, equal volume of protein and reservoir solution, the latter containing 30% PEG 4000, 100 mM Tris-HCl, pH 7.4, 100 mM MgCl2, 1 week, against the reservoir well solution additionally with 20% glycerol before data collection, X-ray diffraction structure determination and analysis at 2.3-2.55 A
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, Lys183 is probably important in maintaining the active site environment
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, Lys183 is probably important in maintaining the active site environment
Olsen, D.B.; Hepburn, T.W.; Moos, M.; Mariano, P.S.; Dunaway-Mariano, D.
Investigation of the Bacillus cereus phosphonoacetaldehyde hydrolase. Evidence for a Schiff base mechanism and sequence analysis of an active-site peptide containing the catalytic lysine residue
The crystal structure of Bacillus cereus phosphonoacetaldehyde hydrolase insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily
Investigation of metal ion binding in phosphonoacetaldehyde hydrolase identifies sequence markers for metal-activated enzymes of the HAD enzyme superfamily
Phosphonoacetate biosynthesis: in vitro detection of a novel NADP(+)-dependent phosphonoacetaldehyde-oxidizing activity in cell-extracts of the marine Roseovarius nubinhibens ISM