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Literature summary for 3.11.1.1 extracted from
- Towards understanding phosphonoacetaldehyde hydrolase: an alternative mechanism involving proton transfer that triggers P-C bond cleavage (2008), Chem. Commun. (Camb. ), 2008, 4162-4164.
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| phosphonoacetaldehyde + H2O | Bacillus cereus | - |
acetaldehyde + phosphate | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus cereus | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 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 | Bacillus cereus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| phosphonoacetaldehyde + H2O | - |
Bacillus cereus | acetaldehyde + phosphate | - |
? | |
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