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Literature summary for 3.1.3.2 extracted from

  • van Herk, T.; Hartog, A.F.; Ruijssenaars, H.J.; Kerkman, R.; Schoemaker, H.E.; Wever, R.
    Optimization of the kinetic resolution of the DL-phosphomonoesters of threonine and serine by random mutagenesis of the acid phosphatase from Salmonella enterica (2007), Adv. Synth. Catal., 349, 1349-1352.
No PubMed abstract available
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Protein Variants

Protein Variants Comment Organism
N151D more effective in the formation of D-serine from O-phospho-DL-serine compared to the wild type enzyme Salmonella enterica
V78L more effective in the formation of D-serine from O-phospho-DL-serine compared to the wild type enzyme Salmonella enterica

Organism

Organism UniProt Comment Textmining
Salmonella enterica
-
 serovar typhimurium LT2
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
O-phospho-DL-serine + H2O
-
 Salmonella enterica D-serine + phosphate
-
 ?
O-phospho-DL-threonine + H2O
-
 Salmonella enterica L-threonine + phosphate
-
 ?
p-nitrophenyl phosphate + H2O
-
 Salmonella enterica p-nitrophenol + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
PhoN-Se
-
 Salmonella enterica

pH Range

pH Minimum pH Maximum Comment Organism
3.9 5
-
 Salmonella enterica

pH Stability

pH Stability pH Stability Maximum Comment Organism
3.3 6.25 activity clearly diminishes at pH 6.25 and no activity is found at pH 3.3 Salmonella enterica