_EC 3.11.1.1 Phosphonoacetaldehyde hydrolase. 9 PDB entries  
EC 3.-.-.- Hydrolases. [21,051 PDB entries]
EC 3.11.-.- Acting on carbon-phosphorus bonds. [13 PDB entries]
EC 3.11.1.- Acting on carbon-phosphorus bonds. [13 PDB entries]
EC 3.11.1.1 Phosphonoacetaldehyde hydrolase. [9 PDB entries]    
1fez

Reaction: Phosphonoacetaldehyde + H(2)O = acetaldehyde + phosphate.
 


Phosphonoacetaldehyde
+ H(2)O
=
acetaldehyde
+
phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): 2-phosphonoacetylaldehyde phosphonohydrolase. Phosphonatase. Phosphonoacetylaldehyde phosphonohydrolase.
Cofactor(s): Mg(2+).
Comments: 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 to break a C-C bond.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 9 PDB entries in enzyme class E.C.3.11.1.1

  PDB code Protein
1fez
The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase complexed with tungstate, a product analog
Source: Bacillus cereus. Organism_taxid: 1396. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (256 residues) CATH domains: 3.40.50.1000 1.10.150.240
1rdf
G50p mutant of phosphonoacetaldehyde hydrolase in complex with substrate analogue vinyl sulfonate
Source: Bacillus cereus. Organism_taxid: 1396. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C, D, E, F (263 residues) CATH domains: 3.40.50.1000 1.10.150.240
1rql
Crystal structure of phosponoacetaldehyde hydrolase complexed with magnesium and the inhibitor vinyl sulfonate
Source: Bacillus cereus. Organism_taxid: 1396. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (257 residues) CATH domains: 3.40.50.1000 1.10.150.240
1rqn
Phosphonoacetaldehyde hydrolase complexed with magnesium
Source: Bacillus cereus. Organism_taxid: 1396. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (257 residues) CATH domains: 3.40.50.1000 1.10.150.240
1swv
Crystal structure of the d12a mutant of phosphonoacetaldehyde hydrolase complexed with magnesium
Source: Bacillus cereus. Organism_taxid: 1396. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (257 residues) CATH domains: 3.40.50.1000 1.10.150.240
1sww
Crystal structure of the phosphonoacetaldehyde hydrolase d12a mutant complexed with magnesium and substrate phosphonoacetaldehyde
Source: Bacillus cereus. Organism_taxid: 1396. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (257 residues) CATH domains: 3.40.50.1000 1.10.150.240
Bound ligand:   Het Group POA corresponds to enzyme reactant 2-phosphonoacetaldehyde
2iof
Crystal structure of phosphonoacetaldehyde hydrolase with sodium borohydride-reduced substrate intermediate
Source: Bacillus cereus. Organism_taxid: 1396. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562
Chains: A, K (256 residues) CATH domains: 3.40.50.1000 1.10.150.240
Bound ligand:   Het Group PO4 corresponds to enzyme product phosphate
2ioh
Crystal structure of phosphonoacetaldehyde hydrolase with a mutation
Source: Bacillus cereus. Organism_taxid: 1396. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C, D (256 residues) CATH domains: 3.40.50.1000 1.10.150.240
Bound ligand:   Het Group PO4 corresponds to enzyme product phosphate
3iru
Crystal structure of phoshonoacetaldehyde hydrolase like pro oleispira antarctica
Source: Oleispira antarctica. Organism_taxid: 188908. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (276 residues) CATH domains: 3.40.50.1000 1.10.150.240