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Literature summary for 1.14.20.1 extracted from

  • Wu, X.B.; Tian, X.Y.; Ji, J.J.; Wu, W.B.; Fan, K.Q.; Yang, K.Q.
    Saturation mutagenesis of Acremonium chrysogenum deacetoxy/deacetylcephalosporin C synthase R308 site confirms its role in controlling substrate specificity (2011), Biotechnol. Lett., 33, 805-812.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
R308A site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Acremonium chrysogenum
R308C site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Acremonium chrysogenum
R308D site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Acremonium chrysogenum
R308E site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Acremonium chrysogenum
R308F site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Acremonium chrysogenum
R308G site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Acremonium chrysogenum
R308H site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Acremonium chrysogenum
R308I site-directed mutagenesis, the mutant shows significant improvement in the ability to convert penicillin analogues compared to the wild-type enzyme. The mutant shows the highest reactivity for penicillin G, with 3fold increase in kcat/Km ratio and 7fold increase in relative activity Acremonium chrysogenum
R308K site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Acremonium chrysogenum
R308L site-directed mutagenesis, the mutant shows significant improvement in the ability to convert penicillin analogues compared to the wild-type enzyme Acremonium chrysogenum
R308M site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Acremonium chrysogenum
R308N site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Acremonium chrysogenum
R308P site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Acremonium chrysogenum
R308Q site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Acremonium chrysogenum
R308S site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Acremonium chrysogenum
R308T site-directed mutagenesis, the mutant shows significant improvement in the ability to convert penicillin analogues compared to the wild-type enzyme Acremonium chrysogenum
R308V site-directed mutagenesis, the mutant shows significant improvement in the ability to convert penicillin analogues compared to the wild-type enzyme Acremonium chrysogenum
R308W site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Acremonium chrysogenum
R308Y site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Acremonium chrysogenum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.9
-
penicillin G wild-type enzyme, pH not specified in the publication, temperature not specified in the publication Acremonium chrysogenum
8.2
-
penicillin G mutant R308I, pH not specified in the publication, temperature not specified in the publication Acremonium chrysogenum
11
-
penicillin G mutant R308L, pH not specified in the publication, temperature not specified in the publication Acremonium chrysogenum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
deacetoxycephalosporin C + 2-oxoglutarate + O2 Acremonium chrysogenum
-
deacetylcephalosporin C + succinate + CO2 + H2O
-
?
additional information Acremonium chrysogenum a bifunctional enzyme that catalyzes both the ring-expansion of penicillin N to deacetoxycephalosporin C and the hydroxylation of the latter to deacetylcephalosporin C ?
-
?
penicillin N + 2-oxoglutarate + O2 Acremonium chrysogenum
-
deacetoxycephalosporin C + succinate + CO2 + H2O
-
?

Organism

Organism UniProt Comment Textmining
Acremonium chrysogenum
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
relative activities of wild-type and R308 mutants with penicillin variants and analogue substrates, overview Acremonium chrysogenum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6-aminopenicillanic acid + 2-oxoglutarate + O2
-
Acremonium chrysogenum ? + succinate + CO2 + H2O
-
?
amoxicillin + 2-oxoglutarate + O2
-
Acremonium chrysogenum ? + succinate + CO2 + H2O
-
?
ampicillin + 2-oxoglutarate + O2
-
Acremonium chrysogenum ? + succinate + CO2 + H2O
-
?
carbenicillin + 2-oxoglutarate + O2
-
Acremonium chrysogenum ? + succinate + CO2 + H2O
-
?
deacetoxycephalosporin C + 2-oxoglutarate + O2
-
Acremonium chrysogenum deacetylcephalosporin C + succinate + CO2 + H2O
-
?
additional information a bifunctional enzyme that catalyzes both the ring-expansion of penicillin N to deacetoxycephalosporin C and the hydroxylation of the latter to deacetylcephalosporin C Acremonium chrysogenum ?
-
?
additional information role of residue R308 in controlling substrate selectivity, substrate specificity of wild-type and mutant enzymes, overview Acremonium chrysogenum ?
-
?
penicillin G + 2-oxoglutarate + O2
-
Acremonium chrysogenum phenylacetyl-7-aminodeacetoxycephalosporanic acid + succinate + CO2 + H2O
-
?
penicillin N + 2-oxoglutarate + O2
-
Acremonium chrysogenum deacetoxycephalosporin C + succinate + CO2 + H2O
-
?
penicillin V + 2-oxoglutarate + O2
-
Acremonium chrysogenum ? + succinate + CO2 + H2O
-
?

Synonyms

Synonyms Comment Organism
acDAOC/DACS
-
Acremonium chrysogenum
deacetoxy/deacetylcephalosporin C synthase
-
Acremonium chrysogenum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0057
-
penicillin G wild-type enzyme, pH not specified in the publication, temperature not specified in the publication Acremonium chrysogenum
0.048
-
penicillin G mutant R308L, pH not specified in the publication, temperature not specified in the publication Acremonium chrysogenum
0.069
-
penicillin G mutant R308I, pH not specified in the publication, temperature not specified in the publication Acremonium chrysogenum

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.003
-
penicillin G wild-type enzyme, pH not specified in the publication, temperature not specified in the publication Acremonium chrysogenum
0.0045
-
penicillin G mutant R308L, pH not specified in the publication, temperature not specified in the publication Acremonium chrysogenum
0.0085
-
penicillin G mutant R308I, pH not specified in the publication, temperature not specified in the publication Acremonium chrysogenum