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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

Reaction

phosphonoacetaldehyde
+
H2O
=
acetaldehyde
 +
phosphate

Synonyms

2-phosphonoacetaldehyde phosphonohydrolase, 2-phosphonoacetylaldehyde phosphonohydrolase, hydrolase, phosphonoacetylaldehyde, P-Ald hydrolase, phosphonatase

ECTree

     3 Hydrolases
         3.11 Acting on carbon-phosphorus bonds
             3.11.1 Acting on carbon-phosphorus bonds (only sub-subclass identified to date)
                3.11.1.1 phosphonoacetaldehyde hydrolase

Crystallization

Crystallization on EC 3.11.1.1 - phosphonoacetaldehyde hydrolase

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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
crystal structure of the homodimeric enzyme complexed with the phosphate analogue tungstate and Mg2+
-
mutant enzymes
-