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Literature summary extracted from

  • Barends, T.R.; Polderman-Tijmes, J.J.; Jekel, P.A.; Williams, C.; Wybenga, G.; Janssen, D.B.; Dijkstra, B.W.
    Acetobacter turbidans alpha -Amino Acid Ester Hydrolase: how a single mutation improves an antibiotic-producing enzyme (2006), J. Biol. Chem., 281, 5804-5810.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.1.43
-
 Acetobacter pasteurianus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.43 S205A inactive mutant Acetobacter pasteurianus
3.1.1.43 Y206A active site mutant with an increased tendency to catalyze antibiotic production rather than hydrolysis Acetobacter pasteurianus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.43 0.45
-
 cephalexin
-
 Acetobacter pasteurianus
3.1.1.43 1
-
 D-phenylglycine methyl ester
-
 Acetobacter pasteurianus

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.43 Acetobacter pasteurianus Q8VRK8
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.43 metal ion affinity chromatography using nickel-nitrilotriacetic acid-Agarose Acetobacter pasteurianus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.43 D-phenylglycine methyl ester + 7-amino-desacetoxycephalosporanic acid
-
 Acetobacter pasteurianus cephalexin + H2O
-
 r

Subunits

EC Number Subunits Comment Organism
3.1.1.43 tetramer
-
 Acetobacter pasteurianus

Synonyms

EC Number Synonyms Comment Organism
3.1.1.43 alpha-amino acid ester hydrolase
-
 Acetobacter pasteurianus