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Literature summary for 3.5.1.93 extracted from

  • Isogai, Y.; Nakayama, K.
    Alteration of substrate selection of antibiotic acylase from beta-lactam to echinocandin (2015), Protein Eng. Des. Sel., 29, 49-56 .
    View publication on PubMed
Search for more literature for 3.5.1.93

Application

Application Comment Organism
synthesis antibiotic acylases are key enzymes for the industrial production of antibiotic drugs Pseudomonas sp. SY-77-1

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) under the control of the T7 promoter Pseudomonas sp. SY-77-1

Protein Variants

Protein Variants Comment Organism
F177betaG site-directed mutagenesis Pseudomonas sp. SY-77-1
F177betaG/M145alphaA site-directed mutagenesis, mutant CAAC1, the mutant has an altered substrate binding site with increased affinity for binding of long acyl chains, it shows altered substrate specificity, lower enzymatic activity with cephalosporin but higher activity with aculeacin A, in comparison with the wild-type enzyme Pseudomonas sp. SY-77-1
F177betaG/M145alphaA site-directed mutagenesis, mutant CAAC2, the mutant has an altered substrate binding site with increased affinity for binding of long acyl chains, it shows altered substrate specificity, lower enzymatic activity with cephalosporin but higher activity with aculeacin A, in comparison with the wild-type enzyme Pseudomonas sp. SY-77-1
F177betaG/M145alphaA/Y149alphaV site-directed mutagenesis, mutant CAAC2, the mutant has an altered substrate binding site with increased affinity for binding of long acyl chains, it shows altered substrate specificity, lower enzymatic activity with cephalosporin but higher activity with aculeacin A, in comparison with the wild-type enzyme Pseudomonas sp. SY-77-1

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
adipyl-7-aminocephalosporanic acid + H2O Pseudomonas sp. SY-77-1
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 7-aminocephalosporanic acid + adipate
-
 ?
glutaryl-7-aminocephalosporanic acid + H2O Pseudomonas sp. SY-77-1
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 7-aminocephalosporanic acid + glutarate
-
 ?
additional information Pseudomonas sp. SY-77-1 a cephalosporin acylase enzyme mutant with binding pocket altered for the binding of long acyl chain shows lower enzymatic activity with cephalosporin but higher activity with aculeacin A, in comparison with the wild-type enzyme ?
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Organism

Organism UniProt Comment Textmining
Pseudomonas sp. SY-77-1 A4ZVL3 i.e. Pseudomonas sp. GK-16
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis Pseudomonas sp. SY-77-1

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
aculeacin A + H2O enzyme binding site mutants CAAC1 and CAAC2, no activity with the wild-type enzyme Pseudomonas sp. SY-77-1 cyclo-hexapeptide + palmitic acid
-
 ?
adipyl-7-aminocephalosporanic acid + H2O
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 Pseudomonas sp. SY-77-1 7-aminocephalosporanic acid + adipate
-
 ?
glutaryl-7-aminocephalosporanic acid + H2O
-
 Pseudomonas sp. SY-77-1 7-aminocephalosporanic acid + glutarate
-
 ?
additional information a cephalosporin acylase enzyme mutant with binding pocket altered for the binding of long acyl chain shows lower enzymatic activity with cephalosporin but higher activity with aculeacin A, in comparison with the wild-type enzyme Pseudomonas sp. SY-77-1 ?
-
-

Synonyms

Synonyms Comment Organism
antibiotic acylase
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 Pseudomonas sp. SY-77-1
cephalosporin acylase
-
 Pseudomonas sp. SY-77-1
glutaryl 7-aminocephalosporanic acid acylase UniProt Pseudomonas sp. SY-77-1

General Information

General Information Comment Organism
evolution the antibiotic acylases belong to the N-terminal nucleophile hydrolase superfamily Pseudomonas sp. SY-77-1
metabolism antibiotic acylases cephalosporin acylase and penicillin G acylase (EC 3.5.1.11) catalyze the deacylation of beta-lactam antibiotics, while aculeacin A acylase (EC 3.5.1.70) is known to be an alternative acylase class catalyzing the deacylation of echinocandin or cyclic lipopeptide antibiotic compounds Pseudomonas sp. SY-77-1
additional information cephalosporin acylase structure, PDB ID 1or0, is used to construct a three-dimensional homology model of aculeacin A acylase (EC 3.5.1.70), and docking simulation with substrate ligands. Cephalosporin acylase mutant has the deep narrow binding pocket for the long-chain fatty acyl group of the echinocandin molecule. Docking study, overview Pseudomonas sp. SY-77-1