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Literature summary 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

EC Number Protein Variants Comment Organism
3.1.1.73 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
3.1.1.73 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.73 0.26
-
 alpha-naphthylbutyrate 37°C, pH 5.0, wild-type enzyme Aspergillus awamori
3.1.1.73 0.28
-
 alpha-naphthylbutyrate 37°C, pH 5.0, mutant enzyme N79Q Aspergillus awamori
3.1.1.73 0.66
-
 alpha-naphthylbutyrate 37°C, pH 5.0, mutant enzyme N79A Aspergillus awamori

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.73 35000
-
 x * 35000, mutant enzyme N79A, SDS-PAGE Aspergillus awamori
3.1.1.73 35000
-
 x * 35000, mutant enzyme N79Q, SDS-PAGE Aspergillus awamori
3.1.1.73 37000
-
 x * 37000, wild-type enzyme, SDS-PAGE Aspergillus awamori

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.73 Aspergillus awamori
-
 NBRC4033
-
3.1.1.73 Aspergillus awamori NBRC4033
-
 NBRC4033
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.1.73 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)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.73 1-naphthyl butyrate + H2O
-
 Aspergillus awamori 1-naphthol + butyrate
-
 ?
3.1.1.73 1-naphthyl butyrate + H2O
-
 Aspergillus awamori NBRC4033 1-naphthol + butyrate
-
 ?
3.1.1.73 1-naphthyl caprylate + H2O
-
 Aspergillus awamori 1-naphthol + caprylate
-
 ?
3.1.1.73 1-naphthyl caprylate + H2O
-
 Aspergillus awamori NBRC4033 1-naphthol + caprylate
-
 ?

Subunits

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.73 45
-
 wild-type enzyme and mutant enzymes N79A and N79Q Aspergillus awamori

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.73 48
-
 T50-value for mutant enzyme N79A is 48.1°C Aspergillus awamori
3.1.1.73 48
-
 T50-value for mutant enzyme N79Q is 47.7°C Aspergillus awamori
3.1.1.73 50
-
 60 min, wild-type enzyme retains 70% of its activity, mutant enzymes N79A and N79Q retain no activity Aspergillus awamori
3.1.1.73 52
-
 T50-value for mutant enzyme is 51.6°C Aspergillus awamori

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.1.73 21
-
 alpha-naphthylbutyrate 37°C, pH 5.0, mutant enzyme N79Q Aspergillus awamori
3.1.1.73 97
-
 alpha-naphthylbutyrate 37°C, pH 5.0, mutant enzyme N79A Aspergillus awamori
3.1.1.73 153
-
 alpha-naphthylbutyrate 37°C, pH 5.0, wild-type enzyme Aspergillus awamori