Crystallization (Comment) | Organism |
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full quantum chemical study performed at the density functional level, based on PDB entry 1HDH. The enzyme is able to catalyze the hydrolysis of the original 4-nitrophenyl sulfate substrate and the promiscuous 4-nitrophenyl phosphate.Only some steps of the promiscuous reaction are identical to those in the native process. Differences concern mainly the last step in which the His115 residue acts as a general base to accept the proton by the O atom of the FGly51 in the 4-nitrophenyl sulfate, whereas in 4-nitrophenyl phosphate, the Asp317 protonated residue works as a general acid to deliver a proton by a water molecule to the oxygen atom of the C-O bond | Pseudomonas aeruginosa |
Organism | UniProt | Comment | Textmining |
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Pseudomonas aeruginosa | P51691 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
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4-nitrophenyl phosphate + H2O | the enzyme is able to catalyze the hydrolysis of the original 4-nitrophenyl sulfate substrate and the promiscuous 4-nitrophenyl phosphate. Only some steps of the promiscuous reaction are identical to those in the native process. Differences concern mainly the last step in which the His115 residue acts as a general base to accept the proton by the O atom of the FGly51 in the 4-nitrophenyl sulfate, whereas in 4-nitrophenyl phosphate, the Asp317 protonated residue works as a general acid to deliver a proton by a water molecule to the oxygen atom of the C-O bond. The rate-determining steps are different in the two reactions, i.e. nucleophile attack vs. nucleophile activation | Pseudomonas aeruginosa | 4-nitrophenol + phosphate | - |
? | |
4-nitrophenyl sulfate + H2O | the enzyme is able to catalyze the hydrolysis of the original 4-nitrophenyl sulfate substrate and the promiscuous 4-nitrophenyl phosphate. Only some steps of the promiscuous reaction are identical to those in the native process. Differences concern mainly the last step in which the His115 residue acts as a general base to accept the proton by the O atom of the FGly51 in the 4-nitrophenyl sulfate, whereas in 4-nitrophenyl phosphate, the Asp317 protonated residue works as a general acid to deliver a proton by a water molecule to the oxygen atom of the C-O bond. The rate-determining steps are different in the two reactions, i.e. nucleophile attack vs. nucleophile activation | Pseudomonas aeruginosa | 4-nitrophenol + sulfate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AtsA | - |
Pseudomonas aeruginosa |