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Literature summary for 3.1.1.20 extracted from

  • Koseki, T.; Otsuka, M.; Mizuno, T.; Shiono, Y.
    Mutational analysis of Kex2 recognition sites and a disulfide bond in tannase from Aspergillus oryzae (2017), Biochem. Biophys. Res. Commun., 482, 1165-1169 .
    View publication on PubMed
Search for more literature for 3.1.1.20

Cloned(Commentary)

Cloned (Comment) Organism
gene tanA, recombinant expression of wild-type and mutant enzymes in Pichia pastoris strain GS115, recombinant AoTanA and its mutant variants are secreted using a Saccharomyces cerevisiae alpha-factor secretion signal peptide fusion, the recombinant proteins accumulate in the culture broth Aspergillus oryzae

Protein Variants

Protein Variants Comment Organism
C194A site-directed mutagenesis, almost inactive mutant Aspergillus oryzae
C502A site-directed mutagenesis, almost inactive mutant Aspergillus oryzae
additional information construction of a seven amino-acid deletion variant of region Lys310eArg316 (mutant DELTAKR). The mutant shows only one band by SDS-PAGE after treatment with endoglycosidase H. The DELTAKR variant exhibits higher activity compared to the wild-type enzyme Aspergillus oryzae
R311A/R316A site-directed mutagenesis, the mutant exhibits the two bands similar to wild-type by SDS-PAGE after treatment with endoglycosidase H. The mutation has no effect on tannase activity and stability Aspergillus oryzae

Organism

Organism UniProt Comment Textmining
Aspergillus oryzae P78581
-
-
Aspergillus oryzae ATCC 42149 P78581
-
-
Aspergillus oryzae RIB 40 P78581
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the enzyme consists of two subunits that are generated by the cleavage of tannase gene product by the Kex2 protease, TanA has two Kex2 recognition sites at positions Arg311 and Arg316 Aspergillus oryzae

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Pichia pastoris strain GS115 by anion exchange chromatography, ultrafiltration, and gel filtration Aspergillus oryzae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(-)-catechin gallate + H2O high activity Aspergillus oryzae (-)-catechin + gallic acid
-
 ?
(-)-catechin gallate + H2O high activity Aspergillus oryzae RIB 40 (-)-catechin + gallic acid
-
 ?
(-)-catechin gallate + H2O high activity Aspergillus oryzae ATCC 42149 (-)-catechin + gallic acid
-
 ?
(-)-epicatechin gallate + H2O best substrate Aspergillus oryzae (-)-epicatechin + gallic acid
-
 ?
(-)-epicatechin gallate + H2O best substrate Aspergillus oryzae RIB 40 (-)-epicatechin + gallic acid
-
 ?
(-)-epicatechin gallate + H2O best substrate Aspergillus oryzae ATCC 42149 (-)-epicatechin + gallic acid
-
 ?
(-)-epigallocatechin gallate + H2O moderate activity Aspergillus oryzae (-)-epigallocatechin + gallic acid
-
 ?
(-)-epigallocatechin gallate + H2O moderate activity Aspergillus oryzae RIB 40 (-)-epigallocatechin + gallic acid
-
 ?
(-)-epigallocatechin gallate + H2O moderate activity Aspergillus oryzae ATCC 42149 (-)-epigallocatechin + gallic acid
-
 ?
ethyl gallate + H2O lower activity Aspergillus oryzae ethanol + gallic acid
-
 ?
ethyl gallate + H2O lower activity Aspergillus oryzae RIB 40 ethanol + gallic acid
-
 ?
ethyl gallate + H2O lower activity Aspergillus oryzae ATCC 42149 ethanol + gallic acid
-
 ?
methyl gallate + H2O moderate activity Aspergillus oryzae methanol + gallic acid
-
 ?
additional information tannase activity is assayed by monitoring the production of gallic acid, released from methyl gallate, through reaction with rhodanine. The enzyme has no activity with the methyl esters of ferulic, p-coumaric, caffeic, and sinapic acids, or with the ethyl, propyl, and butyl esters of 4-hydroxybenzoic acid. Substrate specificity, overview Aspergillus oryzae ?
-
 ?
additional information tannase activity is assayed by monitoring the production of gallic acid, released from methyl gallate, through reaction with rhodanine. The enzyme has no activity with the methyl esters of ferulic, p-coumaric, caffeic, and sinapic acids, or with the ethyl, propyl, and butyl esters of 4-hydroxybenzoic acid. Substrate specificity, overview Aspergillus oryzae RIB 40 ?
-
 ?
additional information tannase activity is assayed by monitoring the production of gallic acid, released from methyl gallate, through reaction with rhodanine. The enzyme has no activity with the methyl esters of ferulic, p-coumaric, caffeic, and sinapic acids, or with the ethyl, propyl, and butyl esters of 4-hydroxybenzoic acid. Substrate specificity, overview Aspergillus oryzae ATCC 42149 ?
-
 ?
propyl gallate + H2O lower activity Aspergillus oryzae propanol + gallic acid
-
 ?

Synonyms

Synonyms Comment Organism
AoTanA
-
 Aspergillus oryzae
TanA
-
 Aspergillus oryzae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Aspergillus oryzae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4
-
 assay at Aspergillus oryzae

General Information

General Information Comment Organism
additional information the catalytic triad residues of AoTanA are predicted to be Ser195, Asp455, and His501, with the serine and histidine residues brought together by a disulfide bond of the neighboring cysteines, Cys194 and Cys502. Functional role of the Kex2 recognition sites and disulfide bond between the neighboring cysteines in enzyme AoTanA, overview Aspergillus oryzae