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Literature summary for 3.1.1.43 extracted from

  • Fernandez-Lafuente, R.; Hernandez-Justiz, O.; Mateo, C.; Terreni, M.; Alonso, J.; Garcia-Lopez, J.L.; Moreno, M.A.; Guisan, J.M.
    Stabilization of a tetrameric enzyme (a-amino acid ester hydrolase from Acetobacter turbidans) enables a very improved performance of ampicillin synthesis (2001), J. Mol. Catal. B, 11, 633-638.
No PubMed abstract available

General Stability

General Stability Organism
soluble enzyme is very rapidly inactivated Acetobacter pasteurianus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
an alpha-aminoacid ester + H2O Acetobacter pasteurianus
-
an alpha-amino acid + an alcohol
-
r

Organism

Organism UniProt Comment Textmining
Acetobacter pasteurianus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Acetobacter pasteurianus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
an alpha-aminoacid ester + H2O
-
Acetobacter pasteurianus an alpha-amino acid + an alcohol
-
?
an alpha-aminoacid ester + H2O
-
Acetobacter pasteurianus an alpha-amino acid + an alcohol
-
r
D-phenylglycine methyl ester + 6-amino penicillanic acid specific for D-isomer Acetobacter pasteurianus ampicillin
-
?
D-phenylglycine methyl ester + H2O
-
Acetobacter pasteurianus D-phenylglycine + methanol
-
?
DL-phenylglycine methyl ester + 6-amino penicillanic acid more than 85% of D-phenylglycine methyl ester is transformed into ampicillin Acetobacter pasteurianus ampicillin
-
?