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Literature summary for 3.5.1.11 extracted from

  • Jager, S.A.; Shapovalova, I.V.; Jekel, P.A.; Alkema, W.B.; Svedas, V.K.; Janssen, D.B.
    Saturation mutagenesis reveals the importance of residues alphaR145 and alphaF146 of penicillin acylase in the synthesis of beta-lactam antibiotics (2008), J. Biotechnol., 133, 18-26.
    View publication on PubMed
Search for more literature for 3.5.1.11

Protein Variants

Protein Variants Comment Organism
F146A mutation in alpha-subunit. 99% of ampicillin synthesis activity compared to wild-type Escherichia coli
F146C mutation in alpha-subunit. 241% of ampicillin synthesis activity compared to wild-type Escherichia coli
F146D mutation in alpha-subunit. No ampicillin synthesis activity Escherichia coli
F146E mutation in alpha-subunit. 13% of ampicillin synthesis activity compared to wild-type Escherichia coli
F146G mutation in alpha-subunit. 61% of ampicillin synthesis activity compared to wild-type Escherichia coli
F146H mutation in alpha-subunit. 174% of ampicillin synthesis activity compared to wild-type Escherichia coli
F146I mutation in alpha-subunit. 135% of ampicillin synthesis activity compared to wild-type Escherichia coli
F146K mutation in alpha-subunit. 120% of ampicillin synthesis activity compared to wild-type Escherichia coli
F146L mutation in alpha-subunit. 169% of ampicillin synthesis activity compared to wild-type Escherichia coli
F146M mutation in alpha-subunit. 85% of ampicillin synthesis activity compared to wild-type Escherichia coli
F146N mutation in alpha-subunit. 151% of ampicillin synthesis activity compared to wild-type Escherichia coli
F146P mutation in alpha-subunit. 112% of ampicillin synthesis activity compared to wild-type Escherichia coli
F146Q mutation in alpha-subunit. 114% of ampicillin synthesis activity compared to wild-type Escherichia coli
F146R mutation in alpha-subunit. 3% of ampicillin synthesis activity compared to wild-type Escherichia coli
F146S mutation in alpha-subunit. 238% of ampicillin synthesis activity compared to wild-type Escherichia coli
F146T mutation in alpha-subunit. 376% of ampicillin synthesis activity compared to wild-type Escherichia coli
F146V mutation in alpha-subunit. 153% of ampicillin synthesis activity compared to wild-type Escherichia coli
F146W mutation in alpha-subunit. 10% of ampicillin synthesis activity compared to wild-type Escherichia coli
F146Y mutation in alpha-subunit. No ampicillin synthesis activity Escherichia coli
R145A mutation in alpha-subunit. 154% of ampicillin synthesis activity compared to wild-type Escherichia coli
R145C mutation in alpha-subunit. 169% of ampicillin synthesis activity compared to wild-type Escherichia coli
R145D mutation in alpha-subunit. 15% of ampicillin synthesis activity compared to wild-type Escherichia coli
R145E mutation in alpha-subunit. 6% of ampicillin synthesis activity compared to wild-type Escherichia coli
R145F mutation in alpha-subunit. 131% of ampicillin synthesis activity compared to wild-type Escherichia coli
R145G mutation in alpha-subunit. 256% of ampicillin synthesis activity compared to wild-type. Due to increased tendency of the acyl-enzyme intermediate to react with beta-lactam nucleophile instead of water, the mutant demonstrates an enhanced synthetic yield over wild-type penicillin acylase at high substrate concentrations. This is accompanied by an increased conversion of 6-aminopenicillanic acid to ampicillin as well as a decreased undesirable hydrolysis of the acyl donor Escherichia coli
R145H mutation in alpha-subunit. 78% of ampicillin synthesis activity compared to wild-type Escherichia coli
R145I mutation in alpha-subunit. 120% of ampicillin synthesis activity compared to wild-type Escherichia coli
R145K mutation in alpha-subunit. 145% of ampicillin synthesis activity compared to wild-type Escherichia coli
R145L mutation in alpha-subunit. 237% of ampicillin synthesis activity compared to wild-type. Due to increased tendency of the acyl-enzyme intermediate to react with beta-lactam nucleophile instead of water, the mutant demonstrates an enhanced synthetic yield over wild-type penicillin acylase at high substrate concentrations. This is accompanied by an increased conversion of 6-aminopenicillanic acid to ampicillin as well as a decreased undesirable hydrolysis of the acyl donor Escherichia coli
R145M mutation in alpha-subunit. 129% of ampicillin synthesis activity compared to wild-type Escherichia coli
R145N mutation in alpha-subunit. 173% of ampicillin synthesis activity compared to wild-type Escherichia coli
R145P mutation in alpha-subunit. 137% of ampicillin synthesis activity compared to wild-type Escherichia coli
R145Q mutation in alpha-subunit. 158% of ampicillin synthesis activity compared to wild-type Escherichia coli
R145S mutation in alpha-subunit. 192% of ampicillin synthesis activity compared to wild-type. Due to increased tendency of the acyl-enzyme intermediate to react with beta-lactam nucleophile instead of water, the mutant demonstrates an enhanced synthetic yield over wild-type penicillin acylase at high substrate concentrations. This is accompanied by an increased conversion of 6-aminopenicillanic acid to ampicillin as well as a decreased undesirable hydrolysis of the acyl donor Escherichia coli
R145T mutation in alpha-subunit. 127% of ampicillin synthesis activity compared to wild-type Escherichia coli
R145V mutation in alpha-subunit. 127% of ampicillin synthesis activity compared to wild-type Escherichia coli
R145W mutation in alpha-subunit. 103% of ampicillin synthesis activity compared to wild-type Escherichia coli
R145Y mutation in alpha-subunit. 37% of ampicillin synthesis activity compared to wild-type Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.9
-
 ampicillin mutant alphaR145L Escherichia coli
2 3 D-phenylglycine amide mutant alphaR145G Escherichia coli
3.6
-
 ampicillin wild-type enzyme Escherichia coli
4.6
-
 ampicillin mutant alphaR145S Escherichia coli
5.2
-
 ampicillin mutant alphaR145G Escherichia coli
9.1
-
 D-phenylglycine amide mutant alphaR145L Escherichia coli
13
-
 D-phenylglycine amide mutant alphaR145S Escherichia coli
27
-
 D-phenylglycine amide wild-type enzyme Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
 Escherichia coli
-
-

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-phenylglycine amide + 6-aminopenicillanic acid
-
 Escherichia coli ampicillin + NH3
-
 r
D-phenylglycine amide + H2O
-
 Escherichia coli D-phenylglycine + NH3
-
 ?

Synonyms

Synonyms Comment Organism
penicillin acylase
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7
-
 D-phenylglycine amide mutant alphaR145S Escherichia coli
3 6 D-phenylglycine amide wild-type enzyme Escherichia coli
3.4
-
 D-phenylglycine amide mutant alphaR145G Escherichia coli
6.8
-
 D-phenylglycine amide mutant alphaR145L Escherichia coli
14
-
 ampicillin mutant alphaR145S Escherichia coli
20
-
 ampicillin mutant alphaR145L Escherichia coli
23
-
 ampicillin mutant alphaR145G Escherichia coli
37
-
 ampicillin wild-type enzyme Escherichia coli