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Literature summary extracted from

  • Kurochkina, V.; Sklyarenko, A.; Berezina, O.; Yarotskii, S.
    alpha-Amino acid ester hydrolases: properties and applications (2013), Appl. Biochem. Microbiol., 49, 672-694.
No PubMed abstract available

Application

EC Number Application Comment Organism
3.1.1.43 synthesis the enzyme catalyzes amino-beta-lactam synthesis, conditions and substrates, overview Xanthomonas sp.
3.1.1.43 synthesis the enzyme catalyzes amino-beta-lactam synthesis, conditions and substrates, overview Acidovorax avenae
3.1.1.43 synthesis the enzyme catalyzes amino-beta-lactam synthesis, conditions and substrates, overview Xanthomonas campestris
3.1.1.43 synthesis the enzyme catalyzes amino-beta-lactam synthesis, conditions and substrates, overview Flavobacterium sp.
3.1.1.43 synthesis the enzyme catalyzes amino-beta-lactam synthesis, conditions and substrates, overview Xanthomonas citri
3.1.1.43 synthesis the enzyme catalyzes amino-beta-lactam synthesis, conditions and substrates, overview Acetobacter pasteurianus
3.1.1.43 synthesis the enzyme catalyzes amino-beta-lactam synthesis, conditions and substrates, overview Xanthomonas oryzae
3.1.1.43 synthesis the enzyme catalyzes amino-beta-lactam synthesis, conditions and substrates, overview Pseudomonas melanogenum

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.43 gene aehA, expression in Escherichia coli Acetobacter pasteurianus
3.1.1.43 gene aehR, expression in Escherichia coli Acidovorax avenae
3.1.1.43 gene aehX, expression in Escherichia coli Xanthomonas citri
3.1.1.43 gene gaa, expression in Escherichia coli Xanthomonas campestris

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.43 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
3.1.1.43 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
3.1.1.43 Y206A the mutant shows 3fold increased cephalexin synthesis activity Xanthomonas citri

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.43 0.00006
-
 valacyclovir pH 7.5, 25°C, recombinant enzyme Rattus norvegicus
3.1.1.43 0.00019
-
 valacyclovir pH 7.4, 37°C, recombinant enzyme Homo sapiens
3.1.1.43 0.00034
-
 cefadroxil pH 6.0, 30°C, recombinant enzyme Acetobacter pasteurianus
3.1.1.43 0.00035
-
 cephalexin pH 6.1, 25°C Xanthomonas sp.
3.1.1.43 0.00059
-
 valacyclovir pH 7.4, 37°C, recombinant enzyme Homo sapiens
3.1.1.43 0.0006
-
 ampicillin pH 6.1, 25°C Xanthomonas sp.
3.1.1.43 0.0006
-
 ampicillin hydrolysis, pH 6.2, 27-30°C Acetobacter pasteurianus
3.1.1.43 0.001
-
 ampicillin pH 6.0, 30°C, recombinant enzyme Acetobacter pasteurianus
3.1.1.43 0.001
-
 cefatrizine below, hydrolysis, pH 6.4, 25°C, recombinant enzyme Xanthomonas citri
3.1.1.43 0.0011
-
 ampicillin pH 7.0, 25°C, recombinant enzyme Xanthomonas campestris
3.1.1.43 0.0012
-
 ampicillin hydrolysis, pH 6.4, 25°C, recombinant enzyme Xanthomonas citri
3.1.1.43 0.0015 0.0037 cephalexin hydrolysis, pH 6.2, 27-30°C Acetobacter pasteurianus
3.1.1.43 0.00161
-
 cephalexin pH 6.0, 37°C Pseudomonas melanogenum
3.1.1.43 0.0017
-
 cefaloglycin pH 6.0, 30°C, recombinant enzyme Acetobacter pasteurianus
3.1.1.43 0.0017
-
 cephalexin hydrolysis, pH 6.2, 35°C, native enzyme Xanthomonas citri
3.1.1.43 0.00179
-
 cefradine pH 6.0, 37°C Pseudomonas melanogenum
3.1.1.43 0.0018
-
 cephalexin hydrolysis, pH 6.4, 25°C, recombinant enzyme Xanthomonas citri
3.1.1.43 0.0019
-
 valganciclovir pH 7.4, 37°C, recombinant enzyme Homo sapiens
3.1.1.43 0.00196
-
 cefaloglycin pH 6.0, 37°C Pseudomonas melanogenum
3.1.1.43 0.0022
-
 cephalexin pH 7.0, 25°C, recombinant enzyme Xanthomonas campestris
3.1.1.43 0.0026
-
 amoxicillin pH 6.0, 30°C, recombinant enzyme Acetobacter pasteurianus
3.1.1.43 0.0026 0.003 D-phenylglycine methyl ester cephalexin synthesis, pH 6.2, 30°C Acetobacter pasteurianus
3.1.1.43 0.003
-
 cephalexin hydrolysis, pH 6.4, 30°C, native enzyme Xanthomonas citri
3.1.1.43 0.0036
-
 D-phenylglycine methyl ester pH 6.1, 25°C Xanthomonas sp.
3.1.1.43 0.0037
-
 D-phenylglycine methyl ester pH 7.0, 25°C, recombinant enzyme Xanthomonas campestris
3.1.1.43 0.004 0.0049 D-phenylglycine methyl ester hydrolysis, pH 6.2, 27-30°C Acetobacter pasteurianus
3.1.1.43 0.00434
-
 ampicillin pH 6.0, 37°C Pseudomonas melanogenum
3.1.1.43 0.0083
-
 D-phenylglycine methyl ester hydrolysis, pH 6.4, 30°C, native enzyme Xanthomonas citri
3.1.1.43 0.0093
-
 cephalexin hydrolysis, pH 6.5, 37°C, native enzyme Xanthomonas citri
3.1.1.43 0.011
-
 4-hydroxy-D-phenylglycine methyl ester pH 6.0, 30°C, recombinant enzyme Acetobacter pasteurianus
3.1.1.43 0.011
-
 D-phenylglycine methyl ester hydrolysis, pH 6.5, 37°C, native enzyme Xanthomonas citri
3.1.1.43 0.013
-
 D-phenylglycine amide above, pH 6.2, 27-30°C Acetobacter pasteurianus
3.1.1.43 0.0145
-
 D-phenylglycine methyl ester cephalexin synthesis, pH 6.4, 30°C, native enzyme Xanthomonas citri
3.1.1.43 0.021
-
 D-phenylglycine methyl ester cephalexin synthesis, pH 6.2, 35°C, native enzyme Xanthomonas citri
3.1.1.43 0.09
-
 D-phenylglycine methyl ester hydrolysis, pH 6.4, 25°C, recombinant enzyme Xanthomonas citri

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.43 27000
-
 2 * 27000 Homo sapiens
3.1.1.43 27000
-
 2 * 27000, in crystals and solution Homo sapiens
3.1.1.43 29000
-
 x * 29000 Rattus norvegicus
3.1.1.43 68000
-
 4 * 68000 Xanthomonas campestris
3.1.1.43 70000
-
 4 * 70000 Xanthomonas sp.
3.1.1.43 70000
-
 2 * 70000, recombinant enzyme Acetobacter pasteurianus
3.1.1.43 70000
-
 4 * 70000, recombinant enzyme Acetobacter pasteurianus
3.1.1.43 70000
-
 alpha2beta2, 2 * 70000 + 2 * 72000 Acetobacter pasteurianus
3.1.1.43 72000
-
 2 * 72000 Pseudomonas melanogenum
3.1.1.43 72000
-
 alpha2beta2, 2 * 70000 + 2 * 72000 Acetobacter pasteurianus
3.1.1.43 146000
-
-
 Pseudomonas melanogenum
3.1.1.43 280000 290000
-
 Acetobacter pasteurianus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.1.43 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 ?
-
 ?
3.1.1.43 additional information Pseudomonas danceae the enzyme synthesizes artificial cephalosporins by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters ?
-
 ?
3.1.1.43 valacyclovir + H2O Rattus norvegicus stereospecific reaction ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.43 Acetobacter pasteurianus
-
-
-
3.1.1.43 Acetobacter pasteurianus
-
 gene aehA
-
3.1.1.43 Acetobacter pasteurianus ATCC 6033
-
-
-
3.1.1.43 Acetobacter pasteurianus ATCC 9325
-
 gene aehA
-
3.1.1.43 Acidovorax avenae
-
-
-
3.1.1.43 Acidovorax avenae
-
 gene aehR
-
3.1.1.43 Acidovorax avenae CGMCC No. 2339
-
-
-
3.1.1.43 Acidovorax avenae VKM B-629
-
-
-
3.1.1.43 Acidovorax avenae VKPMB-9915
-
 gene aehR
-
3.1.1.43 Flavobacterium sp.
-
-
-
3.1.1.43 Flavobacterium sp. ATCC 9325
-
-
-
3.1.1.43 Gluconobacter oxydans
-
-
-
3.1.1.43 Gluconobacter oxydans ATCC 621
-
-
-
3.1.1.43 Homo sapiens
-
-
-
3.1.1.43 Mycoplana dimorpha
-
-
-
3.1.1.43 Mycoplana dimorpha IFO 13213
-
-
-
3.1.1.43 Protaminobacter alboflavus
-
-
-
3.1.1.43 Protaminobacter alboflavus IFO 13221
-
-
-
3.1.1.43 Pseudomonas danceae
-
-
-
3.1.1.43 Pseudomonas melanogenum
-
-
-
3.1.1.43 Pseudomonas melanogenum
-
 a beta-lactamase deficient mutant strain
-
3.1.1.43 Pseudomonas melanogenum ATCC 17808
-
-
-
3.1.1.43 Pseudomonas melanogenum IFO 12020
-
-
-
3.1.1.43 Pseudomonas melanogenum KY3987
-
-
-
3.1.1.43 Pseudomonas melanogenum KY8540
-
 a beta-lactamase deficient mutant strain
-
3.1.1.43 Rattus norvegicus
-
-
-
3.1.1.43 Xanthomonas campestris
-
 pv. campestris, gene gaa
-
3.1.1.43 Xanthomonas campestris IFO 3835
-
 pv. campestris, gene gaa
-
3.1.1.43 Xanthomonas citri
-
 gene aehX
-
3.1.1.43 Xanthomonas citri IFO 3835
-
 gene aehX
-
3.1.1.43 Xanthomonas oryzae
-
-
-
3.1.1.43 Xanthomonas oryzae IFO 3995
-
-
-
3.1.1.43 Xanthomonas sp.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.43 from liver Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.43 breast carcinoma cell
-
 Homo sapiens
-
3.1.1.43 Caco-2 cell
-
 Homo sapiens
-
3.1.1.43 colon carcinoma cell
-
 Homo sapiens
-
3.1.1.43 liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.43 4-hydroxy-D-phenylglycine methyl ester + H2O
-
 Xanthomonas citri 4-hydroxy-D-phenylglycine + methanol
-
 ?
3.1.1.43 4-hydroxy-D-phenylglycine methyl ester + H2O
-
 Acetobacter pasteurianus 4-hydroxy-D-phenylglycine + methanol
-
 ?
3.1.1.43 amoxicillin + H2O
-
 Xanthomonas citri D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid
-
 ?
3.1.1.43 amoxicillin + H2O
-
 Acetobacter pasteurianus D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid
-
 ?
3.1.1.43 amoxicillin + H2O
-
 Xanthomonas citri IFO 3835 D-4-hydroxyphenylglycine amide + 6-aminopenicillanic acid
-
 ?
3.1.1.43 ampicillin + H2O
-
 Xanthomonas sp. (R)-2-phenylglycine + 6-aminopenicillanic acid
-
 ?
3.1.1.43 ampicillin + H2O
-
 Xanthomonas campestris (R)-2-phenylglycine + 6-aminopenicillanic acid
-
 ?
3.1.1.43 ampicillin + H2O
-
 Acetobacter pasteurianus (R)-2-phenylglycine + 6-aminopenicillanic acid
-
 ?
3.1.1.43 ampicillin + H2O binding structure, modeling Xanthomonas citri (R)-2-phenylglycine + 6-aminopenicillanic acid
-
 ?
3.1.1.43 ampicillin + H2O the enzyme catalyzes ampicillin synthesis and hydrolysis Flavobacterium sp. (R)-2-phenylglycine + 6-aminopenicillanic acid
-
 ?
3.1.1.43 ampicillin + H2O the enzyme catalyzes ampicillin synthesis and hydrolysis Pseudomonas melanogenum (R)-2-phenylglycine + 6-aminopenicillanic acid
-
 ?
3.1.1.43 ampicillin + H2O
-
 Xanthomonas campestris IFO 3835 (R)-2-phenylglycine + 6-aminopenicillanic acid
-
 ?
3.1.1.43 ampicillin + H2O the enzyme catalyzes ampicillin synthesis and hydrolysis Pseudomonas melanogenum KY3987 (R)-2-phenylglycine + 6-aminopenicillanic acid
-
 ?
3.1.1.43 ampicillin + H2O the enzyme catalyzes ampicillin synthesis and hydrolysis Flavobacterium sp. ATCC 9325 (R)-2-phenylglycine + 6-aminopenicillanic acid
-
 ?
3.1.1.43 ampicillin + H2O the enzyme catalyzes ampicillin synthesis and hydrolysis Pseudomonas melanogenum IFO 12020 (R)-2-phenylglycine + 6-aminopenicillanic acid
-
 ?
3.1.1.43 ampicillin + H2O the enzyme catalyzes ampicillin synthesis and hydrolysis Pseudomonas melanogenum ATCC 17808 (R)-2-phenylglycine + 6-aminopenicillanic acid
-
 ?
3.1.1.43 ampicillin + H2O the enzyme catalyzes ampicillin synthesis and hydrolysis Pseudomonas melanogenum KY8540 (R)-2-phenylglycine + 6-aminopenicillanic acid
-
 ?
3.1.1.43 ampicillin + H2O binding structure, modeling Xanthomonas citri IFO 3835 (R)-2-phenylglycine + 6-aminopenicillanic acid
-
 ?
3.1.1.43 cefadroxil + H2O
-
 Acetobacter pasteurianus ?
-
 ?
3.1.1.43 cefadroxil + H2O
-
 Acetobacter pasteurianus ATCC 6033 ?
-
 ?
3.1.1.43 cefadroxil + H2O
-
 Acetobacter pasteurianus ATCC 9325 ?
-
 ?
3.1.1.43 cefaloglycin + H2O
-
 Acetobacter pasteurianus ?
-
 ?
3.1.1.43 cefaloglycin + H2O hydrolysis Pseudomonas melanogenum ?
-
 ?
3.1.1.43 cefatrizine + H2O
-
 Xanthomonas citri ?
-
 ?
3.1.1.43 cefradine + H2O hydrolysis Pseudomonas melanogenum ?
-
 ?
3.1.1.43 cephalexin + H2O
-
 Xanthomonas sp. D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
 ?
3.1.1.43 cephalexin + H2O
-
 Acidovorax avenae D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
 ?
3.1.1.43 cephalexin + H2O
-
 Xanthomonas campestris D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
 ?
3.1.1.43 cephalexin + H2O
-
 Xanthomonas citri D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
 ?
3.1.1.43 cephalexin + H2O
-
 Acetobacter pasteurianus D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
 ?
3.1.1.43 cephalexin + H2O the enzyme catalyzes cephalexin synthesis and hydrolysis Pseudomonas melanogenum D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
 ?
3.1.1.43 cephalexin + H2O
-
 Xanthomonas campestris IFO 3835 D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
 ?
3.1.1.43 cephalexin + H2O the enzyme catalyzes cephalexin synthesis and hydrolysis Pseudomonas melanogenum KY3987 D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
 ?
3.1.1.43 cephalexin + H2O
-
 Acidovorax avenae VKPMB-9915 D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
 ?
3.1.1.43 cephalexin + H2O the enzyme catalyzes cephalexin synthesis and hydrolysis Pseudomonas melanogenum IFO 12020 D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
 ?
3.1.1.43 cephalexin + H2O the enzyme catalyzes cephalexin synthesis and hydrolysis Pseudomonas melanogenum ATCC 17808 D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
 ?
3.1.1.43 cephalexin + H2O
-
 Acidovorax avenae CGMCC No. 2339 D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
 ?
3.1.1.43 cephalexin + H2O the enzyme catalyzes cephalexin synthesis and hydrolysis Pseudomonas melanogenum KY8540 D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
 ?
3.1.1.43 cephalexin + H2O
-
 Acidovorax avenae VKM B-629 D-phenylglycine + 7-aminodesacetoxycephalosporanic acid
-
 ?
3.1.1.43 D-phenylglycine amide + H2O
-
 Xanthomonas citri D-phenylglycine + NH3
-
 ?
3.1.1.43 D-phenylglycine amide + H2O
-
 Acetobacter pasteurianus D-phenylglycine + NH3
-
 ?
3.1.1.43 D-phenylglycine amide + H2O
-
 Acetobacter pasteurianus ATCC 6033 D-phenylglycine + NH3
-
 ?
3.1.1.43 D-phenylglycine amide + H2O
-
 Acetobacter pasteurianus ATCC 9325 D-phenylglycine + NH3
-
 ?
3.1.1.43 D-phenylglycine amide + H2O
-
 Xanthomonas citri IFO 3835 D-phenylglycine + NH3
-
 ?
3.1.1.43 D-phenylglycine methyl ester + H2O
-
 Xanthomonas sp. D-phenylglycine + methanol
-
 ?
3.1.1.43 D-phenylglycine methyl ester + H2O
-
 Xanthomonas campestris D-phenylglycine + methanol
-
 ?
3.1.1.43 D-phenylglycine methyl ester + H2O
-
 Xanthomonas citri D-phenylglycine + methanol
-
 ?
3.1.1.43 D-phenylglycine methyl ester + H2O
-
 Acetobacter pasteurianus D-phenylglycine + methanol
-
 ?
3.1.1.43 D-phenylglycine methyl ester + H2O
-
 Xanthomonas campestris IFO 3835 D-phenylglycine + methanol
-
 ?
3.1.1.43 D-phenylglycine methyl ester + H2O
-
 Acetobacter pasteurianus ATCC 6033 D-phenylglycine + methanol
-
 ?
3.1.1.43 D-phenylglycine methyl ester + H2O
-
 Acetobacter pasteurianus ATCC 9325 D-phenylglycine + methanol
-
 ?
3.1.1.43 D-phenylglycine methyl ester + H2O
-
 Xanthomonas citri IFO 3835 D-phenylglycine + methanol
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 additional information the enzyme synthesizes artificial cephalosporins by acylating the 7-amino group of cephalosporin nuclei with different alpha-amino acid esters Pseudomonas danceae ?
-
 ?
3.1.1.43 additional information enzyme-mediated hydrolysis of L- and D-isomers of valine esters of a nucleoside-floxuridine Homo sapiens ?
-
 ?
3.1.1.43 additional information the enzyme catalyzes the synthesis of amoxicillin, ampicillin, cephalexin, cefaloglycin, and cefadroxil Pseudomonas melanogenum ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 additional information the enzyme catalyzes the synthesis of amoxicillin, ampicillin, cephalexin, cefaloglycin, and cefadroxil Pseudomonas melanogenum KY3987 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 additional information the enzyme catalyzes the synthesis of amoxicillin, ampicillin, cephalexin, cefaloglycin, and cefadroxil Pseudomonas melanogenum IFO 12020 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 additional information the enzyme catalyzes the synthesis of amoxicillin, ampicillin, cephalexin, cefaloglycin, and cefadroxil Pseudomonas melanogenum ATCC 17808 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 additional information the enzyme catalyzes the synthesis of amoxicillin, ampicillin, cephalexin, cefaloglycin, and cefadroxil Pseudomonas melanogenum KY8540 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 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 ?
-
 ?
3.1.1.43 valacyclovir + H2O
-
 Homo sapiens ?
-
 ?
3.1.1.43 valacyclovir + H2O stereospecific reaction Rattus norvegicus ?
-
 ?
3.1.1.43 valacyclovir + H2O stereospecific reaction, the L-isomer is hydrolyzed approximately 20fold faster than the D-isomer Homo sapiens ?
-
 ?
3.1.1.43 valganciclovir + H2O
-
 Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.43 dimer 2 * 27000 Homo sapiens
3.1.1.43 dimer 2 * 27000, in crystals and solution Homo sapiens
3.1.1.43 dimer 2 * 70000, recombinant enzyme Acetobacter pasteurianus
3.1.1.43 homodimer 2 * 72000 Pseudomonas melanogenum
3.1.1.43 homotetramer 4 * 70000 Xanthomonas sp.
3.1.1.43 homotetramer 4 * 68000 Xanthomonas campestris
3.1.1.43 homotetramer 4 * 70000, recombinant enzyme Acetobacter pasteurianus
3.1.1.43 homotetramer 4 * 70000-72000 Acidovorax avenae
3.1.1.43 homotetramer 4 * 71000-72000 Xanthomonas citri
3.1.1.43 monomer or dimer x * 29000 Rattus norvegicus
3.1.1.43 tetramer alpha2beta2, 2 * 70000 + 2 * 72000 Acetobacter pasteurianus

Synonyms

EC Number Synonyms Comment Organism
3.1.1.43 AEH
-
 Homo sapiens
3.1.1.43 AEH
-
 Rattus norvegicus
3.1.1.43 AEH
-
 Xanthomonas sp.
3.1.1.43 AEH
-
 Acidovorax avenae
3.1.1.43 AEH
-
 Xanthomonas campestris
3.1.1.43 AEH
-
 Gluconobacter oxydans
3.1.1.43 AEH
-
 Flavobacterium sp.
3.1.1.43 AEH
-
 Xanthomonas citri
3.1.1.43 AEH
-
 Acetobacter pasteurianus
3.1.1.43 AEH
-
 Mycoplana dimorpha
3.1.1.43 AEH
-
 Protaminobacter alboflavus
3.1.1.43 AEH
-
 Xanthomonas oryzae
3.1.1.43 AEH
-
 Pseudomonas melanogenum
3.1.1.43 AEH
-
 Pseudomonas danceae
3.1.1.43 alpha-amino acid ester hydrolase
-
 Homo sapiens
3.1.1.43 alpha-amino acid ester hydrolase
-
 Rattus norvegicus
3.1.1.43 alpha-amino acid ester hydrolase
-
 Xanthomonas sp.
3.1.1.43 alpha-amino acid ester hydrolase
-
 Acidovorax avenae
3.1.1.43 alpha-amino acid ester hydrolase
-
 Xanthomonas campestris
3.1.1.43 alpha-amino acid ester hydrolase
-
 Gluconobacter oxydans
3.1.1.43 alpha-amino acid ester hydrolase
-
 Flavobacterium sp.
3.1.1.43 alpha-amino acid ester hydrolase
-
 Xanthomonas citri
3.1.1.43 alpha-amino acid ester hydrolase
-
 Acetobacter pasteurianus
3.1.1.43 alpha-amino acid ester hydrolase
-
 Mycoplana dimorpha
3.1.1.43 alpha-amino acid ester hydrolase
-
 Protaminobacter alboflavus
3.1.1.43 alpha-amino acid ester hydrolase
-
 Xanthomonas oryzae
3.1.1.43 alpha-amino acid ester hydrolase
-
 Pseudomonas melanogenum
3.1.1.43 alpha-amino acid ester hydrolase
-
 Pseudomonas danceae
3.1.1.43 biphenyl hydrolase-like protein
-
 Homo sapiens
3.1.1.43 BPH
-
 Homo sapiens
3.1.1.43 VACVase
-
 Homo sapiens
3.1.1.43 VACVase
-
 Rattus norvegicus
3.1.1.43 valacyclovirase
-
 Homo sapiens
3.1.1.43 valacyclovirase
-
 Rattus norvegicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.43 25 37 broad optimum Homo sapiens
3.1.1.43 25 37 broad optimum Rattus norvegicus
3.1.1.43 30
-
 assay at Pseudomonas melanogenum
3.1.1.43 35 45
-
 Xanthomonas sp.
3.1.1.43 35 45
-
 Acidovorax avenae
3.1.1.43 35 45
-
 Xanthomonas campestris
3.1.1.43 35 45
-
 Gluconobacter oxydans
3.1.1.43 35 45
-
 Flavobacterium sp.
3.1.1.43 35 45
-
 Xanthomonas citri
3.1.1.43 35 45
-
 Acetobacter pasteurianus
3.1.1.43 35 45
-
 Mycoplana dimorpha
3.1.1.43 35 45
-
 Protaminobacter alboflavus
3.1.1.43 35 45
-
 Xanthomonas oryzae
3.1.1.43 35 45
-
 Pseudomonas melanogenum
3.1.1.43 35 45
-
 Pseudomonas danceae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.1.43 1.6
-
 D-phenylglycine amide hydrolysis, pH 6.4, 25°C, recombinant enzyme Xanthomonas citri
3.1.1.43 2.3
-
 cefatrizine hydrolysis, pH 6.4, 25°C, recombinant enzyme Xanthomonas citri
3.1.1.43 9.6
-
 cefaloglycin pH 6.0, 30°C, recombinant enzyme Acetobacter pasteurianus
3.1.1.43 10
-
 amoxicillin pH 6.0, 30°C, recombinant enzyme Acetobacter pasteurianus
3.1.1.43 17.5
-
 ampicillin pH 6.1, 25°C Xanthomonas sp.
3.1.1.43 43
-
 D-phenylglycine amide above, pH 6.2, 27-30°C Acetobacter pasteurianus
3.1.1.43 58
-
 ampicillin hydrolysis, pH 6.4, 25°C, recombinant enzyme Xanthomonas citri
3.1.1.43 71
-
 cephalexin pH 6.1, 25°C Xanthomonas sp.
3.1.1.43 72.5
-
 ampicillin pH 7.0, 25°C, recombinant enzyme Xanthomonas campestris
3.1.1.43 79
-
 valacyclovir pH 7.4, 37°C, recombinant enzyme Homo sapiens
3.1.1.43 101
-
 valganciclovir pH 7.4, 37°C, recombinant enzyme Homo sapiens
3.1.1.43 126
-
 valacyclovir pH 7.4, 37°C, recombinant enzyme Homo sapiens
3.1.1.43 160
-
 cephalexin hydrolysis, pH 6.4, 25°C, recombinant enzyme Xanthomonas citri
3.1.1.43 162
-
 ampicillin hydrolysis, pH 6.2, 27-30°C Acetobacter pasteurianus
3.1.1.43 162
-
 ampicillin pH 6.0, 30°C, recombinant enzyme Acetobacter pasteurianus
3.1.1.43 200
-
 cephalexin pH 7.0, 25°C, recombinant enzyme Xanthomonas campestris
3.1.1.43 263
-
 4-hydroxy-D-phenylglycine methyl ester pH 6.0, 30°C, recombinant enzyme Acetobacter pasteurianus
3.1.1.43 347
-
 cefadroxil pH 6.0, 30°C, recombinant enzyme Acetobacter pasteurianus
3.1.1.43 982
-
 D-phenylglycine methyl ester pH 7.0, 25°C, recombinant enzyme Xanthomonas campestris
3.1.1.43 1000
-
 D-phenylglycine methyl ester pH 6.1, 25°C Xanthomonas sp.
3.1.1.43 1035
-
 D-phenylglycine methyl ester hydrolysis, pH 6.2, 27-30°C Acetobacter pasteurianus
3.1.1.43 1100
-
 D-phenylglycine methyl ester hydrolysis, pH 6.4, 30°C, native enzyme Xanthomonas citri
3.1.1.43 1860
-
 D-phenylglycine methyl ester hydrolysis, pH 6.4, 25°C, recombinant enzyme Xanthomonas citri
3.1.1.43 3200
-
 cephalexin hydrolysis, pH 6.4, 30°C, native enzyme Xanthomonas citri

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.43 5.5 6 strain KY3987, ampicillin synthesis Pseudomonas melanogenum
3.1.1.43 6 6.5
-
 Gluconobacter oxydans
3.1.1.43 6 6.5
-
 Acetobacter pasteurianus
3.1.1.43 6 6.5
-
 Mycoplana dimorpha
3.1.1.43 6 6.5
-
 Protaminobacter alboflavus
3.1.1.43 6 6.5
-
 Xanthomonas oryzae
3.1.1.43 6 6.5
-
 Pseudomonas danceae
3.1.1.43 6
-
 ampicillin synthesis and hydrolysis Pseudomonas melanogenum
3.1.1.43 6 6.4 synthesis and hydrolysis of cephalexin and D-phenylglycine methyl ester Xanthomonas citri
3.1.1.43 6.1 6.2 synthesis and hydrolysis of cephalexin and D-phenylglycine methyl ester Xanthomonas sp.
3.1.1.43 6.2
-
 cephalexin synthesis and hydrolysis Acetobacter pasteurianus
3.1.1.43 6.5
-
 assay at Pseudomonas melanogenum
3.1.1.43 6.5
-
 cephalexin hydrolysis Acidovorax avenae
3.1.1.43 6.5
-
 strain KY3987, synthesis of amoxicillin, ampicillin, cephalexin, cefaloglycin, and cefadroxil Pseudomonas melanogenum
3.1.1.43 6.5
-
 strain KY8540, synthesis of amoxicillin, ampicillin, cephalexin, cefaloglycin, and cefadroxil Pseudomonas melanogenum
3.1.1.43 6.8
-
 ampicillin hydrolysis Xanthomonas campestris
3.1.1.43 7.4
-
 valacyclovir hydrolysis in vitro Homo sapiens
3.1.1.43 7.4 8 valacyclovir hydrolysis in vitro Homo sapiens
3.1.1.43 7.5
-
 ampicillin synthesis and hydrolysis, no hydrolysis of penicillin G Flavobacterium sp.
3.1.1.43 7.5
-
 valacyclovir hydrolysis in vitro Rattus norvegicus

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.1.1.43 Acetobacter pasteurianus
-
-
 5.8
3.1.1.43 Acidovorax avenae
-
-
 6.8
3.1.1.43 Pseudomonas melanogenum
-
-
 7.2
3.1.1.43 Xanthomonas sp.
-
-
 7.6
3.1.1.43 Xanthomonas campestris
-
-
 7.8
3.1.1.43 Xanthomonas citri
-
-
 7.8
3.1.1.43 Homo sapiens above
-
 8
3.1.1.43 Rattus norvegicus
-
-
 9.4

General Information

EC Number General Information Comment Organism
3.1.1.43 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
3.1.1.43 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
3.1.1.43 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.
3.1.1.43 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
3.1.1.43 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
3.1.1.43 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
3.1.1.43 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
3.1.1.43 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
3.1.1.43 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
3.1.1.43 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
3.1.1.43 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
3.1.1.43 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
3.1.1.43 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.
3.1.1.43 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
3.1.1.43 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
3.1.1.43 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
3.1.1.43 additional information the catalytic triad is formed by residues Serl22, Asp227, and His255, catalysis involves residues Asp123 and Met52 Homo sapiens
3.1.1.43 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
3.1.1.43 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
3.1.1.43 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
3.1.1.43 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
3.1.1.43 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
3.1.1.43 additional information the enzyme from strain IFO 12020 contains two active site His residues per subunit Pseudomonas melanogenum

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.1.1.43 3.3
-
 D-phenylglycine amide above, pH 6.2, 27-30°C Acetobacter pasteurianus
3.1.1.43 3.9
-
 amoxicillin pH 6.0, 30°C, recombinant enzyme Acetobacter pasteurianus
3.1.1.43 6
-
 cefaloglycin pH 6.0, 30°C, recombinant enzyme Acetobacter pasteurianus
3.1.1.43 24
-
 4-hydroxy-D-phenylglycine methyl ester pH 6.0, 30°C, recombinant enzyme Acetobacter pasteurianus
3.1.1.43 30
-
 ampicillin pH 6.1, 25°C Xanthomonas sp.
3.1.1.43 53
-
 valganciclovir pH 7.4, 37°C, recombinant enzyme Homo sapiens
3.1.1.43 64.5
-
 ampicillin pH 7.0, 25°C, recombinant enzyme Xanthomonas campestris
3.1.1.43 95
-
 cephalexin pH 7.0, 25°C, recombinant enzyme Xanthomonas campestris
3.1.1.43 148
-
 D-phenylglycine methyl ester hydrolysis, pH 6.2, 27-30°C Acetobacter pasteurianus
3.1.1.43 162
-
 ampicillin hydrolysis, pH 6.0, 30°C Acetobacter pasteurianus
3.1.1.43 200
-
 cephalexin pH 6.1, 25°C Xanthomonas sp.
3.1.1.43 213
-
 valacyclovir pH 7.4, 37°C, recombinant enzyme Homo sapiens
3.1.1.43 265
-
 D-phenylglycine methyl ester pH 7.0, 25°C, recombinant enzyme Xanthomonas campestris
3.1.1.43 280
-
 D-phenylglycine methyl ester pH 6.1, 25°C Xanthomonas sp.
3.1.1.43 420
-
 valacyclovir pH 7.4, 37°C, recombinant enzyme Homo sapiens
3.1.1.43 1021
-
 cefadroxil pH 6.0, 30°C, recombinant enzyme Acetobacter pasteurianus
3.1.1.43 1100
-
 cephalexin hydrolysis, pH 6.4, 30°C, native enzyme Xanthomonas citri
3.1.1.43 1300
-
 D-phenylglycine methyl ester hydrolysis, pH 6.4, 30°C, native enzyme Xanthomonas citri