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Literature summary for 3.1.1.10 extracted from

  • Van der Drift, A.C.M; Beck, H.C.; Dekker, W.H.; Hulst, A.G.; Wils, E.R.J.
    31P NMR and mass spectrometry of atropinesterase and some serine proteases phosphorylated with a transition-state analogue (1985), Biochemistry, 24, 6894-6903.
    View publication on PubMed
Search for more literature for 3.1.1.10

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
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 PMBL-1
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Pseudomonas putida PMBL-1
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 PMBL-1
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
atropine + H2O
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 Pseudomonas putida tropine + tropate
-
 ?
atropine + H2O
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 Pseudomonas putida PMBL-1 tropine + tropate
-
 ?
additional information the active center region in AtrE resembles that of serine proteases with regard to the so-called charge-relay system, the oxyanion hole and the nonpolar binding crevice, suggesting that esterolysis by the enzyme proceeds according to a mechanism similar to that of proteolysis by alpha-chymotrypsin or subtilisin A Pseudomonas putida ?
-
 ?
additional information the active center region in AtrE resembles that of serine proteases with regard to the so-called charge-relay system, the oxyanion hole and the nonpolar binding crevice, suggesting that esterolysis by the enzyme proceeds according to a mechanism similar to that of proteolysis by alpha-chymotrypsin or subtilisin A Pseudomonas putida PMBL-1 ?
-
 ?