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Literature summary for 3.1.1.43 extracted from
- Changing the specificity of alpha-amino acid ester hydrolase toward para-hydroxyl cephalosporins synthesis by site-directed saturation mutagenesis (2012), Biotechnol. Lett., 34, 1719-1724.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overexpression of wild-type and mutant enzymes in Escherichia coli | Acidovorax avenae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | based on the crystal structure of the AEH and cefprozil complex, 13 residues not directly involved in substrate recognition are mutated individually, mutant screening for activity using cefprozil as a model product, overview | Acidovorax avenae |
| R87I | site-directed saturation mutagenesis | Acidovorax avenae |
| V131S | site-directed saturation mutagenesis | Acidovorax avenae |
| V131S | site-directed saturation mutagenesis, the mutant shows the highest initial rates of synthesis toward three p-hydroxyl cephalosporins with 23%, 17% and 64% increases in maximum product accumulation of cefadroxil, cefprozil and cefatrizine, respectively | Acidovorax avenae |
| Y175A | site-directed saturation mutagenesis | Acidovorax avenae |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 63 | - |
D-4-hydroxyphenylglycine methyl ester | mutant V1318S, pH 6.2, 30°C | Acidovorax avenae |  |
| 64 | - |
D-4-hydroxyphenylglycine methyl ester | mutant R87I, pH 6.2, 30°C | Acidovorax avenae | |
| 82 | - |
D-4-hydroxyphenylglycine methyl ester | wild-type enzyme, pH 6.2, 30°C | Acidovorax avenae | |
| 292 | - |
D-4-hydroxyphenylglycine methyl ester | mutant V175A, pH 6.2, 30°C | Acidovorax avenae | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Acidovorax avenae | alpha-amino acid ester hydrolase catalyzes the synthesis of beta-lactam antibiotics, e.g. cefadroxil, cefprozil and cefatrizine, containing an alpha-amino group with decreased activity toward antibiotics with a para-hydroxyl group | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acidovorax avenae | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-4-hydroxyphenylglycine methyl ester + H2O | - |
Acidovorax avenae | D-4-hydroxyphenylglycine + methanol | - |
? | |
| additional information | alpha-amino acid ester hydrolase catalyzes the synthesis of beta-lactam antibiotics, e.g. cefadroxil, cefprozil and cefatrizine, containing an alpha-amino group with decreased activity toward antibiotics with a para-hydroxyl group | Acidovorax avenae | ? | - |
? | |
| additional information | synthesis of artificial cephalosporins by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters, e.g. synthesis of cefprozil, cefatrizine, and cefadroxil from D-4-hydroxyphenylglycine methyl ester or D-oxyphenylglycine methyl ester and 7-amino-3-propenylcephalosporanic acid, 7-amino-3-[(1H-1,2,3-triazol-4-ylthio)methyl]-cephalosporanic acid, or 7-amino-3-desacetoxy cephalosporanic acid, substrate specificity of wild-type and mutant enzymes, overview | Acidovorax avenae | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AEH | - |
Acidovorax avenae |
| alpha-amino acid ester hydrolase | - |
Acidovorax avenae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Acidovorax avenae |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 147 | - |
D-4-hydroxyphenylglycine methyl ester | wild-type enzyme, pH 6.2, 30°C | Acidovorax avenae | |
| 262 | - |
D-4-hydroxyphenylglycine methyl ester | mutant R87I, pH 6.2, 30°C | Acidovorax avenae | |
| 605 | - |
D-4-hydroxyphenylglycine methyl ester | mutant V1318S, pH 6.2, 30°C | Acidovorax avenae | |
| 613 | - |
D-4-hydroxyphenylglycine methyl ester | mutant V175A, pH 6.2, 30°C | Acidovorax avenae | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.2 | - |
assay at | Acidovorax avenae |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | the catalytic triad is formed by residues S174, D307, and H340, and the conserved residue Y82 participates in stabilization of the oxyanion hole | Acidovorax avenae |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0018 | - |
D-4-hydroxyphenylglycine methyl ester | wild-type enzyme, pH 6.2, 30°C | Acidovorax avenae | |
| 0.0021 | - |
D-4-hydroxyphenylglycine methyl ester | mutant V175A, pH 6.2, 30°C | Acidovorax avenae | |
| 0.0041 | - |
D-4-hydroxyphenylglycine methyl ester | mutant R87I, pH 6.2, 30°C | Acidovorax avenae | |
| 0.0096 | - |
D-4-hydroxyphenylglycine methyl ester | mutant V1318S, pH 6.2, 30°C | Acidovorax avenae | |
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