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Literature summary for 3.1.1.43 extracted from

  • Sklyarenko, A.; Berezina, O.; Satarova, D.; Fedorchuk, V.; Fedorchuk, E.; Savin, S.; Yarotsky, S.; Tishkov, V.
    Recombinant alpha-amino ester acid hydrolase from Xanthomonas rubrilineans VKPM B-9915 is a highly efficient biocatalyst of cephalexin synthesis (2014), Moscow Univ. Chem. Bull., 69, 62-67.
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
ethylene glycol addition of ethylene glycol at 33 vol% to the reaction medium for cephalexin synthesis improves the yield from 70% to 95% Acidovorax avenae

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression in Escherichia coli strain VKPM B-11246 Acidovorax avenae

Protein Variants

Protein Variants Comment Organism
additional information synthesis of amino-betalactam antibiotic cephalexin by the recombinant enzyme produced in Escherichia coli VKPM B-11246 is more efficient in comparison with the wild-type enzyme prepared from mutant strain Xanthomonas rubrilineans VKPM B-9915. Addition of ethylene glycol at 33 vol% to the reaction medium for cephalexin synthesis improves the yield from 70% to 95% Acidovorax avenae

Organism

Organism UniProt Comment Textmining
Acidovorax avenae
-
-
-
Acidovorax avenae VKPM B-9915
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme possesses high specificity to esters containing an amino group as a substituent on the Calpha atom of the acid, and it is capable to catalyze N-acylation of 7-aminocephem and 6-aminopenam by these esters with the formation of an amide bond. Synthesis of amino-beta-lactam antibiotic cephalexin from the key intermediate 7-aminodesacetoxycephalosporanic acid and the acylating agent of D-phenylglycine methyl ester by the recombinant enzyme in cell-free extract produced in Escherichia coli VKPM B-11246 is more efficient in comparison with the wild-type enzyme in cell-free extract prepared from mutant strain Xanthomonas rubrilineans VKPM B-9915 Acidovorax avenae ?
-
?
additional information the enzyme possesses high specificity to esters containing an amino group as a substituent on the Calpha atom of the acid, and it is capable to catalyze N-acylation of 7-aminocephem and 6-aminopenam by these esters with the formation of an amide bond. Synthesis of amino-beta-lactam antibiotic cephalexin from the key intermediate 7-aminodesacetoxycephalosporanic acid and the acylating agent of D-phenylglycine methyl ester by the recombinant enzyme in cell-free extract produced in Escherichia coli VKPM B-11246 is more efficient in comparison with the wild-type enzyme in cell-free extract prepared from mutant strain Xanthomonas rubrilineans VKPM B-9915 Acidovorax avenae VKPM B-9915 ?
-
?

Synonyms

Synonyms Comment Organism
AEH
-
Acidovorax avenae
alpha-amino acid ester hydrolase
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Acidovorax avenae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
assay at Acidovorax avenae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 6.25 assay at Acidovorax avenae

General Information

General Information Comment Organism
evolution the enzyme belongs to the class of hydrolases with alpha/beta-type folding Acidovorax avenae