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Literature summary for 3.5.1.11 extracted from

  • Chandel, A.K.; Rao, L.V.; Narasu, M.L.; Singh, O.V.
    The realm of penicillin G acylase in beta-lactam antibiotics (2008), Enzyme Microb. Technol., 42, 199-207.
No PubMed abstract available
Search for more literature for 3.5.1.11

Protein Variants

Protein Variants Comment Organism
C290C 20% decrease in production of penicillin G acylase activity Escherichia coli
F146L mutation in alpha-subunit,3fold increase in transferase/hydrolase ratio using 6-aminopenicillanic acid as nucleophile Escherichia coli
F146W mutation in alpha-subunit, 40fold decrease in transferase/hydrolase ratio using 6-aminopenicillanic acid as nucleophile Escherichia coli
F146Y mutation in alpha-subunit, 40fold decrease in transferase/hydrolase ratio using 6-aminopenicillanic acid as nucleophile Escherichia coli
F24A mutation in beta-subunit, 3fold increase in transferase/hydrolase ratio using 6-aminopenicillanic acid as nucleophile Escherichia coli
F24A mutation in the beta-subunit produces a protein with a higher synthesis/hydrolysis ratio, increased acylase activity, and more resistance to inhibition by phenyl acetic acid Escherichia coli
F71C mutation in B-subunit shows a 100fold increase in kcat/Km towards glutaryl-L-leucine Escherichia coli
F71L mutation in B-subunit shows a 100fold increase in kcat/Km towards glutaryl-L-leucine Escherichia coli
K299H mutant shows very low processing and 90% loss of activity Escherichia coli
K299Q mutant enzyme shows no processing Escherichia coli
K299S mutant enzyme shows no processing Escherichia coli
K427A mutation in beta-chain. Half-life is improved by 60% compared to wild-type enzyme Priestia megaterium
K427A mutation in beta-chain. Mutant shows a great stability to organic solvents Priestia megaterium
K430A mutation in beta-chain. Half-life is improved by 166% compared to wild-type enzyme Priestia megaterium
K430A mutation in beta-chain. Mutant shows a good stability to solvent and thermostability Priestia megaterium
K430A/K427A mutation in beta-chain. Mutant shows a good stability to solvent and thermostability Priestia megaterium
additional information transversion mutation of thymine to guanine at position 1163 results in 90% and 50% of activity loss in penicillin G acylase activity on penicillin G and phenylacetyl-L-leucine respectively Kluyvera cryocrescens
T289C production of penicillin G acylase activity is 92% improved Escherichia coli
T289G production of penicillin G acylase activity is 20% improved Escherichia coli
T289S production of penicillin G acylase activity is 85% improved Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Kluyvera cryocrescens
-
-
-
Priestia megaterium
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
penicillin G + H2O
-
 Kluyvera cryocrescens 6-aminopenicillanic acid + phenylacetic acid
-
 ?
phenylacetyl-L-leucine + H2O
-
 Kluyvera cryocrescens ?
-
 ?

Synonyms

Synonyms Comment Organism
penicillin G acylase
-
 Escherichia coli
penicillin G acylase
-
 Priestia megaterium
penicillin G acylase
-
 Kluyvera cryocrescens