Literature summary for 3.1.1.43 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.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Acetobacter pasteurianus

Protein Variants

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

KM Value [mM]

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

Organism

Organism	UniProt	Comment	Textmining
Acetobacter pasteurianus	Q8VRK8	-	-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
tetramer	-	Acetobacter pasteurianus

Synonyms

Synonyms	Comment	Organism
alpha-amino acid ester hydrolase	-	Acetobacter pasteurianus

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Release 2023.1 (January 2023)