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Literature summary for 3.1.1.73 extracted from

  • Koseki, T.; Takahashi, K.; Handa, T.; Yamane, Y.; Fushinobu, S.; Hashizume, K.
    N-linked oligosaccharides of Aspergillus awamori feruloyl esterase are important for thermostability and catalysis (2006), Biosci. Biotechnol. Biochem., 70, 2476-2480.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
N79A glycosylation-free mutant enzyme has lower activity than that of the recombinant wild-type enzyme towards alpha-naphthylbutyrate, alpha-naphthylcaprylate, and phenolic acid methyl esters. The lower catalytic efficiency is due to a combination of increased KM and decreased kcat. the mutant enzyme exhibits considerably reduced thermostaility relative to wild-type Aspergillus awamori
N79Q glycosylation-free mutant enzyme has lower activity than that of the recombinant wild-type enzyme towards alpha-naphthylbutyrate, alpha-naphthylcaprylate, and phenolic acid methyl esters. The lower catalytic efficiency is due to a considerably decreased kcat. the mutant enzyme exhibits considerably reduced thermostability relative to wild-type Aspergillus awamori

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.26
-
alpha-naphthylbutyrate 37°C, pH 5.0, wild-type enzyme Aspergillus awamori
0.28
-
alpha-naphthylbutyrate 37°C, pH 5.0, mutant enzyme N79Q Aspergillus awamori
0.66
-
alpha-naphthylbutyrate 37°C, pH 5.0, mutant enzyme N79A Aspergillus awamori

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
x * 35000, mutant enzyme N79A, SDS-PAGE Aspergillus awamori
35000
-
x * 35000, mutant enzyme N79Q, SDS-PAGE Aspergillus awamori
37000
-
x * 37000, wild-type enzyme, SDS-PAGE Aspergillus awamori

Organism

Organism UniProt Comment Textmining
Aspergillus awamori
-
NBRC4033
-
Aspergillus awamori NBRC4033
-
NBRC4033
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the native enzyme possesses N-linked oligosaccharides. the recombinant enzyme has a greater mannose content than the wild-type enzyme Aspergillus awamori

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutant enzymes N79A and N79Q Aspergillus awamori

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-naphthyl butyrate + H2O
-
Aspergillus awamori 1-naphthol + butyrate
-
?
1-naphthyl butyrate + H2O
-
Aspergillus awamori NBRC4033 1-naphthol + butyrate
-
?
1-naphthyl caprylate + H2O
-
Aspergillus awamori 1-naphthol + caprylate
-
?
1-naphthyl caprylate + H2O
-
Aspergillus awamori NBRC4033 1-naphthol + caprylate
-
?

Subunits

Subunits Comment Organism
? x * 35000, mutant enzyme N79A, SDS-PAGE Aspergillus awamori
? x * 35000, mutant enzyme N79Q, SDS-PAGE Aspergillus awamori
? x * 37000, wild-type enzyme, SDS-PAGE Aspergillus awamori

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
wild-type enzyme and mutant enzymes N79A and N79Q Aspergillus awamori

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
48
-
T50-value for mutant enzyme N79A is 48.1°C Aspergillus awamori
48
-
T50-value for mutant enzyme N79Q is 47.7°C Aspergillus awamori
50
-
60 min, wild-type enzyme retains 70% of its activity, mutant enzymes N79A and N79Q retain no activity Aspergillus awamori
52
-
T50-value for mutant enzyme is 51.6°C Aspergillus awamori

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
21
-
alpha-naphthylbutyrate 37°C, pH 5.0, mutant enzyme N79Q Aspergillus awamori
97
-
alpha-naphthylbutyrate 37°C, pH 5.0, mutant enzyme N79A Aspergillus awamori
153
-
alpha-naphthylbutyrate 37°C, pH 5.0, wild-type enzyme Aspergillus awamori