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Literature summary for 3.1.1.43 extracted from
- alpha-Amino acid ester hydrolases: properties and applications (2013), Appl. Biochem. Microbiol., 49, 672-694.
No PubMed abstract available
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | the enzyme catalyzes amino-beta-lactam synthesis, conditions and substrates, overview | Xanthomonas sp. |
| synthesis | the enzyme catalyzes amino-beta-lactam synthesis, conditions and substrates, overview | Acidovorax avenae |
| synthesis | the enzyme catalyzes amino-beta-lactam synthesis, conditions and substrates, overview | Xanthomonas campestris |
| synthesis | the enzyme catalyzes amino-beta-lactam synthesis, conditions and substrates, overview | Flavobacterium sp. |
| synthesis | the enzyme catalyzes amino-beta-lactam synthesis, conditions and substrates, overview | Xanthomonas citri |
| synthesis | the enzyme catalyzes amino-beta-lactam synthesis, conditions and substrates, overview | Acetobacter pasteurianus |
| synthesis | the enzyme catalyzes amino-beta-lactam synthesis, conditions and substrates, overview | Xanthomonas oryzae |
| synthesis | the enzyme catalyzes amino-beta-lactam synthesis, conditions and substrates, overview | Pseudomonas melanogenum |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene aehA, expression in Escherichia coli | Acetobacter pasteurianus |
| gene aehR, expression in Escherichia coli | Acidovorax avenae |
| gene aehX, expression in Escherichia coli | Xanthomonas citri |
| gene gaa, expression in Escherichia coli | Xanthomonas campestris |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | Xanthomonas citri strain K24, a beta-lactamase deficient IFO 3835 mutant strain is active at pH 6.0-7.0 in cephalexin synthesis in 5% vol 2-butanol | Xanthomonas campestris |
| additional information | Xanthomonas citri strain K24, a beta-lactamase deficient IFO 3835 mutant strain is active at pH 6.0-7.0 in cephalexin synthesis in 5% vol 2-butanol | Xanthomonas citri |
| Y206A | the mutant shows 3fold increased cephalexin synthesis activity | Xanthomonas citri |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00006 | - |
valacyclovir | pH 7.5, 25°C, recombinant enzyme | Rattus norvegicus |  |
| 0.00019 | - |
valacyclovir | pH 7.4, 37°C, recombinant enzyme | Homo sapiens | |
| 0.00034 | - |
cefadroxil | pH 6.0, 30°C, recombinant enzyme | Acetobacter pasteurianus | |
| 0.00035 | - |
cephalexin | pH 6.1, 25°C | Xanthomonas sp. | |
| 0.00059 | - |
valacyclovir | pH 7.4, 37°C, recombinant enzyme | Homo sapiens | |
| 0.0006 | - |
ampicillin | pH 6.1, 25°C | Xanthomonas sp. | |
| 0.0006 | - |
ampicillin | hydrolysis, pH 6.2, 27-30°C | Acetobacter pasteurianus | |
| 0.001 | - |
ampicillin | pH 6.0, 30°C, recombinant enzyme | Acetobacter pasteurianus | |
| 0.001 | - |
cefatrizine | below, hydrolysis, pH 6.4, 25°C, recombinant enzyme | Xanthomonas citri | |
| 0.0011 | - |
ampicillin | pH 7.0, 25°C, recombinant enzyme | Xanthomonas campestris | |
| 0.0012 | - |
ampicillin | hydrolysis, pH 6.4, 25°C, recombinant enzyme | Xanthomonas citri | |
| 0.0015 | 0.0037 | cephalexin | hydrolysis, pH 6.2, 27-30°C | Acetobacter pasteurianus | |
| 0.00161 | - |
cephalexin | pH 6.0, 37°C | Pseudomonas melanogenum | |
| 0.0017 | - |
cefaloglycin | pH 6.0, 30°C, recombinant enzyme | Acetobacter pasteurianus | |
| 0.0017 | - |
cephalexin | hydrolysis, pH 6.2, 35°C, native enzyme | Xanthomonas citri | |
| 0.00179 | - |
cefradine | pH 6.0, 37°C | Pseudomonas melanogenum | |
| 0.0018 | - |
cephalexin | hydrolysis, pH 6.4, 25°C, recombinant enzyme | Xanthomonas citri | |
| 0.0019 | - |
valganciclovir | pH 7.4, 37°C, recombinant enzyme | Homo sapiens | |
| 0.00196 | - |
cefaloglycin | pH 6.0, 37°C | Pseudomonas melanogenum | |
| 0.0022 | - |
cephalexin | pH 7.0, 25°C, recombinant enzyme | Xanthomonas campestris | |
| 0.0026 | - |
amoxicillin | pH 6.0, 30°C, recombinant enzyme | Acetobacter pasteurianus | |
| 0.0026 | 0.003 | D-phenylglycine methyl ester | cephalexin synthesis, pH 6.2, 30°C | Acetobacter pasteurianus | |
| 0.003 | - |
cephalexin | hydrolysis, pH 6.4, 30°C, native enzyme | Xanthomonas citri | |
| 0.0036 | - |
D-phenylglycine methyl ester | pH 6.1, 25°C | Xanthomonas sp. | |
| 0.0037 | - |
D-phenylglycine methyl ester | pH 7.0, 25°C, recombinant enzyme | Xanthomonas campestris | |
| 0.004 | 0.0049 | D-phenylglycine methyl ester | hydrolysis, pH 6.2, 27-30°C | Acetobacter pasteurianus | |
| 0.00434 | - |
ampicillin | pH 6.0, 37°C | Pseudomonas melanogenum | |
| 0.0083 | - |
D-phenylglycine methyl ester | hydrolysis, pH 6.4, 30°C, native enzyme | Xanthomonas citri | |
| 0.0093 | - |
cephalexin | hydrolysis, pH 6.5, 37°C, native enzyme | Xanthomonas citri | |
| 0.011 | - |
4-hydroxy-D-phenylglycine methyl ester | pH 6.0, 30°C, recombinant enzyme | Acetobacter pasteurianus | |
| 0.011 | - |
D-phenylglycine methyl ester | hydrolysis, pH 6.5, 37°C, native enzyme | Xanthomonas citri | |
| 0.013 | - |
D-phenylglycine amide | above, pH 6.2, 27-30°C | Acetobacter pasteurianus | |
| 0.0145 | - |
D-phenylglycine methyl ester | cephalexin synthesis, pH 6.4, 30°C, native enzyme | Xanthomonas citri | |
| 0.021 | - |
D-phenylglycine methyl ester | cephalexin synthesis, pH 6.2, 35°C, native enzyme | Xanthomonas citri | |
| 0.09 | - |
D-phenylglycine methyl ester | hydrolysis, pH 6.4, 25°C, recombinant enzyme | Xanthomonas citri | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 27000 | - |
2 * 27000 | Homo sapiens |
| 27000 | - |
2 * 27000, in crystals and solution | Homo sapiens |
| 29000 | - |
x * 29000 | Rattus norvegicus |
| 68000 | - |
4 * 68000 | Xanthomonas campestris |
| 70000 | - |
4 * 70000 | Xanthomonas sp. |
| 70000 | - |
2 * 70000, recombinant enzyme | Acetobacter pasteurianus |
| 70000 | - |
4 * 70000, recombinant enzyme | Acetobacter pasteurianus |
| 70000 | - |
alpha2beta2, 2 * 70000 + 2 * 72000 | Acetobacter pasteurianus |
| 72000 | - |
2 * 72000 | Pseudomonas melanogenum |
| 72000 | - |
alpha2beta2, 2 * 70000 + 2 * 72000 | Acetobacter pasteurianus |
| 146000 | - |
- |
Pseudomonas melanogenum |
| 280000 | 290000 | - |
Acetobacter pasteurianus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Rattus norvegicus | substrate specificity of the enzyme, which hydrolyzes valacyclovir and some other aciclovir esters with an alpha-amino group in the acyl radical | ? | - |
? | |
| additional information | Pseudomonas danceae | the enzyme synthesizes artificial cephalosporins by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters | ? | - |
? | |
| valacyclovir + H2O | Rattus norvegicus | stereospecific reaction | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acetobacter pasteurianus | - |
- |
- |
| Acetobacter pasteurianus | - |
gene aehA | - |
| Acetobacter pasteurianus ATCC 6033 | - |
- |
- |
| Acetobacter pasteurianus ATCC 9325 | - |
gene aehA | - |
| Acidovorax avenae | - |
- |
- |
| Acidovorax avenae | - |
gene aehR | - |
| Acidovorax avenae CGMCC No. 2339 | - |
- |
- |
| Acidovorax avenae VKM B-629 | - |
- |
- |
| Acidovorax avenae VKPMB-9915 | - |
gene aehR | - |
| Flavobacterium sp. | - |
- |
- |
| Flavobacterium sp. ATCC 9325 | - |
- |
- |
| Gluconobacter oxydans | - |
- |
- |
| Gluconobacter oxydans ATCC 621 | - |
- |
- |
| Homo sapiens | - |
- |
- |
| Mycoplana dimorpha | - |
- |
- |
| Mycoplana dimorpha IFO 13213 | - |
- |
- |
| Protaminobacter alboflavus | - |
- |
- |
| Protaminobacter alboflavus IFO 13221 | - |
- |
- |
| Pseudomonas danceae | - |
- |
- |
| Pseudomonas melanogenum | - |
- |
- |
| Pseudomonas melanogenum | - |
a beta-lactamase deficient mutant strain | - |
| Pseudomonas melanogenum ATCC 17808 | - |
- |
- |
| Pseudomonas melanogenum IFO 12020 | - |
- |
- |
| Pseudomonas melanogenum KY3987 | - |
- |
- |
| Pseudomonas melanogenum KY8540 | - |
a beta-lactamase deficient mutant strain | - |
| Rattus norvegicus | - |
- |
- |
| Xanthomonas campestris | - |
pv. campestris, gene gaa | - |
| Xanthomonas campestris IFO 3835 | - |
pv. campestris, gene gaa | - |
| Xanthomonas citri | - |
gene aehX | - |
| Xanthomonas citri IFO 3835 | - |
gene aehX | - |
| Xanthomonas oryzae | - |
- |
- |
| Xanthomonas oryzae IFO 3995 | - |
- |
- |
| Xanthomonas sp. | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| from liver | Rattus norvegicus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| breast carcinoma cell | - |
Homo sapiens | - |
| Caco-2 cell | - |
Homo sapiens | - |
| colon carcinoma cell | - |
Homo sapiens | - |
| liver | - |
Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-hydroxy-D-phenylglycine methyl ester + H2O | - |
Xanthomonas citri | 4-hydroxy-D-phenylglycine + methanol | - |
? | |
| 4-hydroxy-D-phenylglycine methyl ester + H2O | - |
Acetobacter pasteurianus | 4-hydroxy-D-phenylglycine + methanol | - |
? | |
| amoxicillin + H2O | - |
Xanthomonas citri | D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid | - |
? | |
| amoxicillin + H2O | - |
Acetobacter pasteurianus | D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid | - |
? | |
| amoxicillin + H2O | - |
Xanthomonas citri IFO 3835 | D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid | - |
? | |
| ampicillin + H2O | - |
Xanthomonas sp. | (R)-2-phenylglycine + 6-aminopenicillanic acid | - |
? | |
| ampicillin + H2O | - |
Xanthomonas campestris | (R)-2-phenylglycine + 6-aminopenicillanic acid | - |
? | |
| ampicillin + H2O | - |
Acetobacter pasteurianus | (R)-2-phenylglycine + 6-aminopenicillanic acid | - |
? | |
| ampicillin + H2O | binding structure, modeling | Xanthomonas citri | (R)-2-phenylglycine + 6-aminopenicillanic acid | - |
? | |
| ampicillin + H2O | the enzyme catalyzes ampicillin synthesis and hydrolysis | Flavobacterium sp. | (R)-2-phenylglycine + 6-aminopenicillanic acid | - |
? | |
| ampicillin + H2O | the enzyme catalyzes ampicillin synthesis and hydrolysis | Pseudomonas melanogenum | (R)-2-phenylglycine + 6-aminopenicillanic acid | - |
? | |
| ampicillin + H2O | - |
Xanthomonas campestris IFO 3835 | (R)-2-phenylglycine + 6-aminopenicillanic acid | - |
? | |
| ampicillin + H2O | the enzyme catalyzes ampicillin synthesis and hydrolysis | Pseudomonas melanogenum KY3987 | (R)-2-phenylglycine + 6-aminopenicillanic acid | - |
? | |
| ampicillin + H2O | the enzyme catalyzes ampicillin synthesis and hydrolysis | Flavobacterium sp. ATCC 9325 | (R)-2-phenylglycine + 6-aminopenicillanic acid | - |
? | |
| ampicillin + H2O | the enzyme catalyzes ampicillin synthesis and hydrolysis | Pseudomonas melanogenum IFO 12020 | (R)-2-phenylglycine + 6-aminopenicillanic acid | - |
? | |
| ampicillin + H2O | the enzyme catalyzes ampicillin synthesis and hydrolysis | Pseudomonas melanogenum ATCC 17808 | (R)-2-phenylglycine + 6-aminopenicillanic acid | - |
? | |
| ampicillin + H2O | the enzyme catalyzes ampicillin synthesis and hydrolysis | Pseudomonas melanogenum KY8540 | (R)-2-phenylglycine + 6-aminopenicillanic acid | - |
? | |
| ampicillin + H2O | binding structure, modeling | Xanthomonas citri IFO 3835 | (R)-2-phenylglycine + 6-aminopenicillanic acid | - |
? | |
| cefadroxil + H2O | - |
Acetobacter pasteurianus | ? | - |
? | |
| cefadroxil + H2O | - |
Acetobacter pasteurianus ATCC 6033 | ? | - |
? | |
| cefadroxil + H2O | - |
Acetobacter pasteurianus ATCC 9325 | ? | - |
? | |
| cefaloglycin + H2O | - |
Acetobacter pasteurianus | ? | - |
? | |
| cefaloglycin + H2O | hydrolysis | Pseudomonas melanogenum | ? | - |
? | |
| cefatrizine + H2O | - |
Xanthomonas citri | ? | - |
? | |
| cefradine + H2O | hydrolysis | Pseudomonas melanogenum | ? | - |
? | |
| cephalexin + H2O | - |
Xanthomonas sp. | D-phenylglycine + 7-aminodesacetoxycephalosporanic acid | - |
? | |
| cephalexin + H2O | - |
Acidovorax avenae | D-phenylglycine + 7-aminodesacetoxycephalosporanic acid | - |
? | |
| cephalexin + H2O | - |
Xanthomonas campestris | D-phenylglycine + 7-aminodesacetoxycephalosporanic acid | - |
? | |
| cephalexin + H2O | - |
Xanthomonas citri | D-phenylglycine + 7-aminodesacetoxycephalosporanic acid | - |
? | |
| cephalexin + H2O | - |
Acetobacter pasteurianus | D-phenylglycine + 7-aminodesacetoxycephalosporanic acid | - |
? | |
| cephalexin + H2O | the enzyme catalyzes cephalexin synthesis and hydrolysis | Pseudomonas melanogenum | D-phenylglycine + 7-aminodesacetoxycephalosporanic acid | - |
? | |
| cephalexin + H2O | - |
Xanthomonas campestris IFO 3835 | D-phenylglycine + 7-aminodesacetoxycephalosporanic acid | - |
? | |
| cephalexin + H2O | the enzyme catalyzes cephalexin synthesis and hydrolysis | Pseudomonas melanogenum KY3987 | D-phenylglycine + 7-aminodesacetoxycephalosporanic acid | - |
? | |
| cephalexin + H2O | - |
Acidovorax avenae VKPMB-9915 | D-phenylglycine + 7-aminodesacetoxycephalosporanic acid | - |
? | |
| cephalexin + H2O | the enzyme catalyzes cephalexin synthesis and hydrolysis | Pseudomonas melanogenum IFO 12020 | D-phenylglycine + 7-aminodesacetoxycephalosporanic acid | - |
? | |
| cephalexin + H2O | the enzyme catalyzes cephalexin synthesis and hydrolysis | Pseudomonas melanogenum ATCC 17808 | D-phenylglycine + 7-aminodesacetoxycephalosporanic acid | - |
? | |
| cephalexin + H2O | - |
Acidovorax avenae CGMCC No. 2339 | D-phenylglycine + 7-aminodesacetoxycephalosporanic acid | - |
? | |
| cephalexin + H2O | the enzyme catalyzes cephalexin synthesis and hydrolysis | Pseudomonas melanogenum KY8540 | D-phenylglycine + 7-aminodesacetoxycephalosporanic acid | - |
? | |
| cephalexin + H2O | - |
Acidovorax avenae VKM B-629 | D-phenylglycine + 7-aminodesacetoxycephalosporanic acid | - |
? | |
| D-phenylglycine amide + H2O | - |
Xanthomonas citri | D-phenylglycine + NH3 | - |
? | |
| D-phenylglycine amide + H2O | - |
Acetobacter pasteurianus | D-phenylglycine + NH3 | - |
? | |
| D-phenylglycine amide + H2O | - |
Acetobacter pasteurianus ATCC 6033 | D-phenylglycine + NH3 | - |
? | |
| D-phenylglycine amide + H2O | - |
Acetobacter pasteurianus ATCC 9325 | D-phenylglycine + NH3 | - |
? | |
| D-phenylglycine amide + H2O | - |
Xanthomonas citri IFO 3835 | D-phenylglycine + NH3 | - |
? | |
| D-phenylglycine methyl ester + H2O | - |
Xanthomonas sp. | D-phenylglycine + methanol | - |
? | |
| D-phenylglycine methyl ester + H2O | - |
Xanthomonas campestris | D-phenylglycine + methanol | - |
? | |
| D-phenylglycine methyl ester + H2O | - |
Xanthomonas citri | D-phenylglycine + methanol | - |
? | |
| D-phenylglycine methyl ester + H2O | - |
Acetobacter pasteurianus | D-phenylglycine + methanol | - |
? | |
| D-phenylglycine methyl ester + H2O | - |
Xanthomonas campestris IFO 3835 | D-phenylglycine + methanol | - |
? | |
| D-phenylglycine methyl ester + H2O | - |
Acetobacter pasteurianus ATCC 6033 | D-phenylglycine + methanol | - |
? | |
| D-phenylglycine methyl ester + H2O | - |
Acetobacter pasteurianus ATCC 9325 | D-phenylglycine + methanol | - |
? | |
| D-phenylglycine methyl ester + H2O | - |
Xanthomonas citri IFO 3835 | D-phenylglycine + methanol | - |
? | |
| additional information | substrate specificity of the enzyme, which hydrolyzes valacyclovir and some other aciclovir esters with an alpha-amino group in the acyl radical | Rattus norvegicus | ? | - |
? | |
| additional information | the enzyme synthesizes artificial cephalosporins by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters | Pseudomonas danceae | ? | - |
? | |
| additional information | enzyme-mediated hydrolysis of L- and D-isomers of valine esters of a nucleoside-floxuridine | Homo sapiens | ? | - |
? | |
| additional information | the enzyme catalyzes the synthesis of amoxicillin, ampicillin, cephalexin, cefaloglycin, and cefadroxil | Pseudomonas melanogenum | ? | - |
? | |
| additional information | the enzyme catalyzes the synthesis of beta-lactam cephalosporin chimeras (6R,7R)-7-(glycylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7R)-7-(D-alanylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7R)-7-(D-leucylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7S)-7-[[(2R)-2-amino-2-phenylacetyl]amino]-8-oxo-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, and (6R,7S)-7-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino]-8-oxo-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, and of amicillin, amoxicillin, cephalexin, cefadroxil cefaloglycin, cefaclor, cefatrizine, cefprozil, cefamandole, procefoperazone, overview | Pseudomonas melanogenum | ? | - |
? | |
| additional information | the enzyme synthesizes ampicillin and artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters | Acetobacter pasteurianus | ? | - |
? | |
| additional information | the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters | Gluconobacter oxydans | ? | - |
? | |
| additional information | the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters | Acetobacter pasteurianus | ? | - |
? | |
| additional information | the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters | Mycoplana dimorpha | ? | - |
? | |
| additional information | the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters | Protaminobacter alboflavus | ? | - |
? | |
| additional information | the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters | Xanthomonas oryzae | ? | - |
? | |
| additional information | the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters | Pseudomonas melanogenum | ? | - |
? | |
| additional information | the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters. No activity of the recombinant enzyme with benzylpenicillin and cefradoxil | Xanthomonas citri | ? | - |
? | |
| additional information | the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters. No activity with benzylpenicillin | Xanthomonas campestris | ? | - |
? | |
| additional information | the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters. No activity with benzylpenicillin | Xanthomonas campestris IFO 3835 | ? | - |
? | |
| additional information | the enzyme catalyzes the synthesis of amoxicillin, ampicillin, cephalexin, cefaloglycin, and cefadroxil | Pseudomonas melanogenum KY3987 | ? | - |
? | |
| additional information | the enzyme catalyzes the synthesis of beta-lactam cephalosporin chimeras (6R,7R)-7-(glycylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7R)-7-(D-alanylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7R)-7-(D-leucylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7S)-7-[[(2R)-2-amino-2-phenylacetyl]amino]-8-oxo-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, and (6R,7S)-7-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino]-8-oxo-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, and of amicillin, amoxicillin, cephalexin, cefadroxil cefaloglycin, cefaclor, cefatrizine, cefprozil, cefamandole, procefoperazone, overview | Pseudomonas melanogenum KY3987 | ? | - |
? | |
| additional information | the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters | Pseudomonas melanogenum KY3987 | ? | - |
? | |
| additional information | the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters | Protaminobacter alboflavus IFO 13221 | ? | - |
? | |
| additional information | the enzyme catalyzes the synthesis of amoxicillin, ampicillin, cephalexin, cefaloglycin, and cefadroxil | Pseudomonas melanogenum IFO 12020 | ? | - |
? | |
| additional information | the enzyme catalyzes the synthesis of beta-lactam cephalosporin chimeras (6R,7R)-7-(glycylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7R)-7-(D-alanylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7R)-7-(D-leucylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7S)-7-[[(2R)-2-amino-2-phenylacetyl]amino]-8-oxo-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, and (6R,7S)-7-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino]-8-oxo-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, and of amicillin, amoxicillin, cephalexin, cefadroxil cefaloglycin, cefaclor, cefatrizine, cefprozil, cefamandole, procefoperazone, overview | Pseudomonas melanogenum IFO 12020 | ? | - |
? | |
| additional information | the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters | Pseudomonas melanogenum IFO 12020 | ? | - |
? | |
| additional information | the enzyme synthesizes ampicillin and artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters | Acetobacter pasteurianus ATCC 6033 | ? | - |
? | |
| additional information | the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters | Acetobacter pasteurianus ATCC 6033 | ? | - |
? | |
| additional information | the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters | Gluconobacter oxydans ATCC 621 | ? | - |
? | |
| additional information | the enzyme catalyzes the synthesis of amoxicillin, ampicillin, cephalexin, cefaloglycin, and cefadroxil | Pseudomonas melanogenum ATCC 17808 | ? | - |
? | |
| additional information | the enzyme catalyzes the synthesis of beta-lactam cephalosporin chimeras (6R,7R)-7-(glycylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7R)-7-(D-alanylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7R)-7-(D-leucylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7S)-7-[[(2R)-2-amino-2-phenylacetyl]amino]-8-oxo-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, and (6R,7S)-7-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino]-8-oxo-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, and of amicillin, amoxicillin, cephalexin, cefadroxil cefaloglycin, cefaclor, cefatrizine, cefprozil, cefamandole, procefoperazone, overview | Pseudomonas melanogenum ATCC 17808 | ? | - |
? | |
| additional information | the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters | Pseudomonas melanogenum ATCC 17808 | ? | - |
? | |
| additional information | the enzyme catalyzes the synthesis of amoxicillin, ampicillin, cephalexin, cefaloglycin, and cefadroxil | Pseudomonas melanogenum KY8540 | ? | - |
? | |
| additional information | the enzyme catalyzes the synthesis of beta-lactam cephalosporin chimeras (6R,7R)-7-(glycylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7R)-7-(D-alanylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7R)-7-(D-leucylamino)-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, (6R,7S)-7-[[(2R)-2-amino-2-phenylacetyl]amino]-8-oxo-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, and (6R,7S)-7-[[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino]-8-oxo-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid, and of amicillin, amoxicillin, cephalexin, cefadroxil cefaloglycin, cefaclor, cefatrizine, cefprozil, cefamandole, procefoperazone, overview | Pseudomonas melanogenum KY8540 | ? | - |
? | |
| additional information | the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters | Pseudomonas melanogenum KY8540 | ? | - |
? | |
| additional information | the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters | Xanthomonas oryzae IFO 3995 | ? | - |
? | |
| additional information | the enzyme synthesizes ampicillin and artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters | Acetobacter pasteurianus ATCC 9325 | ? | - |
? | |
| additional information | the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters | Acetobacter pasteurianus ATCC 9325 | ? | - |
? | |
| additional information | the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters. No activity of the recombinant enzyme with benzylpenicillin and cefradoxil | Xanthomonas citri IFO 3835 | ? | - |
? | |
| additional information | the enzyme synthesizes artificial cephalosporins cephalexin and cefadroxil by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters | Mycoplana dimorpha IFO 13213 | ? | - |
? | |
| valacyclovir + H2O | - |
Homo sapiens | ? | - |
? | |
| valacyclovir + H2O | stereospecific reaction | Rattus norvegicus | ? | - |
? | |
| valacyclovir + H2O | stereospecific reaction, the L-isomer is hydrolyzed approximately 20fold faster than the D-isomer | Homo sapiens | ? | - |
? | |
| valganciclovir + H2O | - |
Homo sapiens | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 27000 | Homo sapiens |
| dimer | 2 * 27000, in crystals and solution | Homo sapiens |
| dimer | 2 * 70000, recombinant enzyme | Acetobacter pasteurianus |
| homodimer | 2 * 72000 | Pseudomonas melanogenum |
| homotetramer | 4 * 70000 | Xanthomonas sp. |
| homotetramer | 4 * 68000 | Xanthomonas campestris |
| homotetramer | 4 * 70000, recombinant enzyme | Acetobacter pasteurianus |
| homotetramer | 4 * 70000-72000 | Acidovorax avenae |
| homotetramer | 4 * 71000-72000 | Xanthomonas citri |
| monomer or dimer | x * 29000 | Rattus norvegicus |
| tetramer | alpha2beta2, 2 * 70000 + 2 * 72000 | Acetobacter pasteurianus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AEH | - |
Homo sapiens |
| AEH | - |
Rattus norvegicus |
| AEH | - |
Xanthomonas sp. |
| AEH | - |
Acidovorax avenae |
| AEH | - |
Xanthomonas campestris |
| AEH | - |
Gluconobacter oxydans |
| AEH | - |
Flavobacterium sp. |
| AEH | - |
Xanthomonas citri |
| AEH | - |
Acetobacter pasteurianus |
| AEH | - |
Mycoplana dimorpha |
| AEH | - |
Protaminobacter alboflavus |
| AEH | - |
Xanthomonas oryzae |
| AEH | - |
Pseudomonas melanogenum |
| AEH | - |
Pseudomonas danceae |
| alpha-amino acid ester hydrolase | - |
Homo sapiens |
| alpha-amino acid ester hydrolase | - |
Rattus norvegicus |
| alpha-amino acid ester hydrolase | - |
Xanthomonas sp. |
| alpha-amino acid ester hydrolase | - |
Acidovorax avenae |
| alpha-amino acid ester hydrolase | - |
Xanthomonas campestris |
| alpha-amino acid ester hydrolase | - |
Gluconobacter oxydans |
| alpha-amino acid ester hydrolase | - |
Flavobacterium sp. |
| alpha-amino acid ester hydrolase | - |
Xanthomonas citri |
| alpha-amino acid ester hydrolase | - |
Acetobacter pasteurianus |
| alpha-amino acid ester hydrolase | - |
Mycoplana dimorpha |
| alpha-amino acid ester hydrolase | - |
Protaminobacter alboflavus |
| alpha-amino acid ester hydrolase | - |
Xanthomonas oryzae |
| alpha-amino acid ester hydrolase | - |
Pseudomonas melanogenum |
| alpha-amino acid ester hydrolase | - |
Pseudomonas danceae |
| biphenyl hydrolase-like protein | - |
Homo sapiens |
| BPH | - |
Homo sapiens |
| VACVase | - |
Homo sapiens |
| VACVase | - |
Rattus norvegicus |
| valacyclovirase | - |
Homo sapiens |
| valacyclovirase | - |
Rattus norvegicus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 37 | broad optimum | Homo sapiens |
| 25 | 37 | broad optimum | Rattus norvegicus |
| 30 | - |
assay at | Pseudomonas melanogenum |
| 35 | 45 | - |
Xanthomonas sp. |
| 35 | 45 | - |
Acidovorax avenae |
| 35 | 45 | - |
Xanthomonas campestris |
| 35 | 45 | - |
Gluconobacter oxydans |
| 35 | 45 | - |
Flavobacterium sp. |
| 35 | 45 | - |
Xanthomonas citri |
| 35 | 45 | - |
Acetobacter pasteurianus |
| 35 | 45 | - |
Mycoplana dimorpha |
| 35 | 45 | - |
Protaminobacter alboflavus |
| 35 | 45 | - |
Xanthomonas oryzae |
| 35 | 45 | - |
Pseudomonas melanogenum |
| 35 | 45 | - |
Pseudomonas danceae |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.6 | - |
D-phenylglycine amide | hydrolysis, pH 6.4, 25°C, recombinant enzyme | Xanthomonas citri | |
| 2.3 | - |
cefatrizine | hydrolysis, pH 6.4, 25°C, recombinant enzyme | Xanthomonas citri | |
| 9.6 | - |
cefaloglycin | pH 6.0, 30°C, recombinant enzyme | Acetobacter pasteurianus | |
| 10 | - |
amoxicillin | pH 6.0, 30°C, recombinant enzyme | Acetobacter pasteurianus | |
| 17.5 | - |
ampicillin | pH 6.1, 25°C | Xanthomonas sp. | |
| 43 | - |
D-phenylglycine amide | above, pH 6.2, 27-30°C | Acetobacter pasteurianus | |
| 58 | - |
ampicillin | hydrolysis, pH 6.4, 25°C, recombinant enzyme | Xanthomonas citri | |
| 71 | - |
cephalexin | pH 6.1, 25°C | Xanthomonas sp. | |
| 72.5 | - |
ampicillin | pH 7.0, 25°C, recombinant enzyme | Xanthomonas campestris | |
| 79 | - |
valacyclovir | pH 7.4, 37°C, recombinant enzyme | Homo sapiens | |
| 101 | - |
valganciclovir | pH 7.4, 37°C, recombinant enzyme | Homo sapiens | |
| 126 | - |
valacyclovir | pH 7.4, 37°C, recombinant enzyme | Homo sapiens | |
| 160 | - |
cephalexin | hydrolysis, pH 6.4, 25°C, recombinant enzyme | Xanthomonas citri | |
| 162 | - |
ampicillin | hydrolysis, pH 6.2, 27-30°C | Acetobacter pasteurianus | |
| 162 | - |
ampicillin | pH 6.0, 30°C, recombinant enzyme | Acetobacter pasteurianus | |
| 200 | - |
cephalexin | pH 7.0, 25°C, recombinant enzyme | Xanthomonas campestris | |
| 263 | - |
4-hydroxy-D-phenylglycine methyl ester | pH 6.0, 30°C, recombinant enzyme | Acetobacter pasteurianus | |
| 347 | - |
cefadroxil | pH 6.0, 30°C, recombinant enzyme | Acetobacter pasteurianus | |
| 982 | - |
D-phenylglycine methyl ester | pH 7.0, 25°C, recombinant enzyme | Xanthomonas campestris | |
| 1000 | - |
D-phenylglycine methyl ester | pH 6.1, 25°C | Xanthomonas sp. | |
| 1035 | - |
D-phenylglycine methyl ester | hydrolysis, pH 6.2, 27-30°C | Acetobacter pasteurianus | |
| 1100 | - |
D-phenylglycine methyl ester | hydrolysis, pH 6.4, 30°C, native enzyme | Xanthomonas citri | |
| 1860 | - |
D-phenylglycine methyl ester | hydrolysis, pH 6.4, 25°C, recombinant enzyme | Xanthomonas citri | |
| 3200 | - |
cephalexin | hydrolysis, pH 6.4, 30°C, native enzyme | Xanthomonas citri | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | 6 | strain KY3987, ampicillin synthesis | Pseudomonas melanogenum |
| 6 | 6.5 | - |
Gluconobacter oxydans |
| 6 | 6.5 | - |
Acetobacter pasteurianus |
| 6 | 6.5 | - |
Mycoplana dimorpha |
| 6 | 6.5 | - |
Protaminobacter alboflavus |
| 6 | 6.5 | - |
Xanthomonas oryzae |
| 6 | 6.5 | - |
Pseudomonas danceae |
| 6 | - |
ampicillin synthesis and hydrolysis | Pseudomonas melanogenum |
| 6 | 6.4 | synthesis and hydrolysis of cephalexin and D-phenylglycine methyl ester | Xanthomonas citri |
| 6.1 | 6.2 | synthesis and hydrolysis of cephalexin and D-phenylglycine methyl ester | Xanthomonas sp. |
| 6.2 | - |
cephalexin synthesis and hydrolysis | Acetobacter pasteurianus |
| 6.5 | - |
assay at | Pseudomonas melanogenum |
| 6.5 | - |
cephalexin hydrolysis | Acidovorax avenae |
| 6.5 | - |
strain KY3987, synthesis of amoxicillin, ampicillin, cephalexin, cefaloglycin, and cefadroxil | Pseudomonas melanogenum |
| 6.5 | - |
strain KY8540, synthesis of amoxicillin, ampicillin, cephalexin, cefaloglycin, and cefadroxil | Pseudomonas melanogenum |
| 6.8 | - |
ampicillin hydrolysis | Xanthomonas campestris |
| 7.4 | - |
valacyclovir hydrolysis in vitro | Homo sapiens |
| 7.4 | 8 | valacyclovir hydrolysis in vitro | Homo sapiens |
| 7.5 | - |
ampicillin synthesis and hydrolysis, no hydrolysis of penicillin G | Flavobacterium sp. |
| 7.5 | - |
valacyclovir hydrolysis in vitro | Rattus norvegicus |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Acetobacter pasteurianus | - |
- |
5.8 |
| Acidovorax avenae | - |
- |
6.8 |
| Pseudomonas melanogenum | - |
- |
7.2 |
| Xanthomonas sp. | - |
- |
7.6 |
| Xanthomonas campestris | - |
- |
7.8 |
| Xanthomonas citri | - |
- |
7.8 |
| Homo sapiens | above | - |
8 |
| Rattus norvegicus | - |
- |
9.4 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Acetobacter pasteurianus belongs to the first group | Acetobacter pasteurianus |
| evolution | two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Acetobacter turbidans belongs to the first group | Acetobacter pasteurianus |
| evolution | two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Flavobacterium sp. belongs to the first group | Flavobacterium sp. |
| evolution | two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Gluconobacter suboxydans belongs to the first group | Gluconobacter oxydans |
| evolution | two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Mycoplana dimorpha belongs to the first group | Mycoplana dimorpha |
| evolution | two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Protaminobacter alboflavus belongs to the first group | Protaminobacter alboflavus |
| evolution | two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Pseudomonas danceae belongs to the first group | Pseudomonas danceae |
| evolution | two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Pseudomonas melanogenum belongs to the first group | Pseudomonas melanogenum |
| evolution | two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas citri belongs to the first group | Xanthomonas campestris |
| evolution | two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas citri belongs to the first group | Xanthomonas citri |
| evolution | two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas oryzae belongs to the first group | Xanthomonas oryzae |
| evolution | two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas rubrilineans belongs to the first group | Acidovorax avenae |
| evolution | two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The enzyme from Xanthomonas sp. belongs to the first group | Xanthomonas sp. |
| evolution | two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The human enzyme belongs to the second group | Homo sapiens |
| evolution | two major groups of alpha-amino acid ester hydrolases contain enzymes with a similar active center structure, which determines their unique specificity to esters containing an amino group in the alpha position to the carbonyl. The first group comprises microbial alpha-amino acid ester hydrolases of the beta-lactam acylase type. Technical biocatalysts based on this group of enzymes are used for the production of semisynthetic amino-beta-lactam antibiotics. The second alpha-amino acid ester hydrolases group includes eukaryotic valacyclovirases, which activate in vivo a number of antiviral and anticancer prodrugs. The rat enzyme belongs to the second group | Rattus norvegicus |
| additional information | the catalytic triad is formed by residues Ser205, Asp338, and His370, the oxyanion hole by residues Tyrll2 andTyr206, and the carboxylate cluster by residues Asp239, Glu340,and Asp341 | Acetobacter pasteurianus |
| additional information | the catalytic triad is formed by residues Serl22, Asp227, and His255, catalysis involves residues Asp123 and Met52 | Homo sapiens |
| additional information | the catalytic triad is formed by residues Serl22, Asp227, and His255, the acyl pocket by the Asp123 side chain and Tyr175, the oxyanion hole by the Asp123 backbone NH group. The enzyme active center contains a large open groove for the leaving alcohol group of the substrate, the nucleoside-containing group in the hydrolysis of valacyclovir and its analogues | Homo sapiens |
| additional information | the catalytic triad is formed by residues Serl74, Asp307, and His340, the oxyanion hole by residues Tyr82 and Tyr175, and the carboxylate cluster by residues Asp208, Glu309, and Asp310. The carboxylate cluster is responsible for the recognition of the substrate alpha-amino group and for binding it by electrostatic interaction | Xanthomonas citri |
| additional information | the catalytic triad is formed by residues Serl74, Asp307, and His340, the oxyanion hole by residues Tyr82 and Tyr175, and the carboxylate cluster by residues Asp208, Glu309, and Asp310. The carboxylate cluster is responsible for the recognition of the substrate alpha-amino group and for binding it by electrostatic interaction, this region affects not only the sub strate specificity of the enzyme but also its activity | Xanthomonas campestris |
| additional information | the catalytic triad is formed by residues Serl75, Asp308, and His341, the oxyanion hole by residues Tyr83 and Tyr176, and the carboxylate cluster by residues Asp209, Glu310, and Asp311 | Acidovorax avenae |
| additional information | the enzyme active center contains a large open groove for the leaving alcohol group of the substrate, the nucleoside-containing group in the hydrolysis of valacyclovir and its analogues | Rattus norvegicus |
| additional information | the enzyme from strain IFO 12020 contains two active site His residues per subunit | Pseudomonas melanogenum |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 3.3 | - |
D-phenylglycine amide | above, pH 6.2, 27-30°C | Acetobacter pasteurianus | |
| 3.9 | - |
amoxicillin | pH 6.0, 30°C, recombinant enzyme | Acetobacter pasteurianus | |
| 6 | - |
cefaloglycin | pH 6.0, 30°C, recombinant enzyme | Acetobacter pasteurianus | |
| 24 | - |
4-hydroxy-D-phenylglycine methyl ester | pH 6.0, 30°C, recombinant enzyme | Acetobacter pasteurianus | |
| 30 | - |
ampicillin | pH 6.1, 25°C | Xanthomonas sp. | |
| 53 | - |
valganciclovir | pH 7.4, 37°C, recombinant enzyme | Homo sapiens | |
| 64.5 | - |
ampicillin | pH 7.0, 25°C, recombinant enzyme | Xanthomonas campestris | |
| 95 | - |
cephalexin | pH 7.0, 25°C, recombinant enzyme | Xanthomonas campestris | |
| 148 | - |
D-phenylglycine methyl ester | hydrolysis, pH 6.2, 27-30°C | Acetobacter pasteurianus | |
| 162 | - |
ampicillin | hydrolysis, pH 6.0, 30°C | Acetobacter pasteurianus | |
| 200 | - |
cephalexin | pH 6.1, 25°C | Xanthomonas sp. | |
| 213 | - |
valacyclovir | pH 7.4, 37°C, recombinant enzyme | Homo sapiens | |
| 265 | - |
D-phenylglycine methyl ester | pH 7.0, 25°C, recombinant enzyme | Xanthomonas campestris | |
| 280 | - |
D-phenylglycine methyl ester | pH 6.1, 25°C | Xanthomonas sp. | |
| 420 | - |
valacyclovir | pH 7.4, 37°C, recombinant enzyme | Homo sapiens | |
| 1021 | - |
cefadroxil | pH 6.0, 30°C, recombinant enzyme | Acetobacter pasteurianus | |
| 1100 | - |
cephalexin | hydrolysis, pH 6.4, 30°C, native enzyme | Xanthomonas citri | |
| 1300 | - |
D-phenylglycine methyl ester | hydrolysis, pH 6.4, 30°C, native enzyme | Xanthomonas citri | |
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Release 2023.1 (January 2023)
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