3.1.1.20: tannase
This is an abbreviated version!
For detailed information about tannase, go to the full flat file.
Word Map on EC 3.1.1.20
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3.1.1.20
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gallic
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tannic
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aspergillus
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niger
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gallate
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plantarum
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submerged
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solid-state
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food industry
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catechin
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pectinase
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biotechnology
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tannery
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gallotannins
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galloylated
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hydrolysable
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paecilomyces
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feruloyl
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tannin-rich
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1-propanol
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depside
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emblica
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pentosus
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synthesis
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variotii
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degradation
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industry
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medicine
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agriculture
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brewing
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nutrition
- 3.1.1.20
-
gallic
-
tannic
- aspergillus
- niger
- gallate
- plantarum
-
submerged
-
solid-state
- food industry
- catechin
- pectinase
- biotechnology
-
tannery
- gallotannins
-
galloylated
-
hydrolysable
-
paecilomyces
-
feruloyl
-
tannin-rich
- 1-propanol
-
depside
- emblica
- pentosus
- synthesis
- variotii
- degradation
- industry
- medicine
- agriculture
- brewing
- nutrition
Reaction
Synonyms
An04g04430, AoTanA, AotanB, ATAN1, depsidase, fungal tannase, gallotannin-degrading esterase, GALLO_1609, LP-tan, plant tannase, TAH, TAH I, TAH II, tan A, Tan410, tan7, TanA, TanB, tanBLP, TanLpl, tannase, tannase I, tannase II, tannin acyl hydrolase, tannin acyl-hydrolase, tannin acylhydrolase, tannin-acyl-hydrolase, TanSg1, yeast tannase
ECTree
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Subunits
Subunits on EC 3.1.1.20 - tannase
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dimer
heterodimer
homodimer
homohexamer
homotetramer
monomer
monomer or dimer
1 or 2 * 50777, the tannase exists as both a dimer and a monomer in solution, calculated from amino acid sequence
oligomer
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x * 30000 + x * 33000, four pairs of two subunits form a hetero-oligomer of a about 300000 Da native tannase, SDS-PAGE
trimer
additional information
?
x * 61700, about, sequence calculation, x * 70000-100000, recombinant glycosylated enzyme, SDS-PAGE, x * 60000-70000, recombinant deglycosylated enzyme, SDS-PAGE
?
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x * 61700, about, sequence calculation, x * 70000-100000, recombinant glycosylated enzyme, SDS-PAGE, x * 60000-70000, recombinant deglycosylated enzyme, SDS-PAGE
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?
Aspergillus niger FGSC A1513
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x * 61700, about, sequence calculation, x * 70000-100000, recombinant glycosylated enzyme, SDS-PAGE, x * 60000-70000, recombinant deglycosylated enzyme, SDS-PAGE
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?
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x * 61700, about, sequence calculation, x * 70000-100000, recombinant glycosylated enzyme, SDS-PAGE, x * 60000-70000, recombinant deglycosylated enzyme, SDS-PAGE
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?
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x * 100000, SDS-PAGE, x * 31000 + x * 34000, SDS-PAGE after treatment with N-glycosidase F, x * 90000, mass spectrometry
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x * 90000-120000, glycosylated extracellular recombinant enzyme, SDS-PAGE, x * 65000, deglycosylated recombinant extracellular enzyme, SDS-PAGE
?
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x * 90000-120000, glycosylated extracellular recombinant enzyme, SDS-PAGE, x * 65000, deglycosylated recombinant extracellular enzyme, SDS-PAGE
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?
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x * 90000-120000, glycosylated extracellular recombinant enzyme, SDS-PAGE, x * 65000, deglycosylated recombinant extracellular enzyme, SDS-PAGE
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1 * 33000 + 1 * 30000, purified tannase digested with N-glycosidase F and loaded with 2-mercaptoethanol, SDS-PAGE
4 * 80000, denatured endogenous and recombinant tannases, SDS-PAGE. 4 * 55000, deglycosylated endogenous and recombinant tannases, SDS-PAGE
homotetramer
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4 * 80000, denatured endogenous and recombinant tannases, SDS-PAGE. 4 * 55000, deglycosylated endogenous and recombinant tannases, SDS-PAGE
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the native enzyme undergoes dissociation into inactive subunits of equal size by treatment with guanidine hydrochloride
additional information
the enzyme contains two structural domains, one with an alpha/beta-hydrolase fold and one lid domain that covers the catalytic site, likely being residues Ser196, Asp448, and His494 the putative catalytic triad, which are connected by a disulfide bond between the neighboring cysteines, Cys195 and Cys495
additional information
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the enzyme contains two structural domains, one with an alpha/beta-hydrolase fold and one lid domain that covers the catalytic site, likely being residues Ser196, Asp448, and His494 the putative catalytic triad, which are connected by a disulfide bond between the neighboring cysteines, Cys195 and Cys495
additional information
-
the enzyme contains two structural domains, one with an alpha/beta-hydrolase fold and one lid domain that covers the catalytic site, likely being residues Ser196, Asp448, and His494 the putative catalytic triad, which are connected by a disulfide bond between the neighboring cysteines, Cys195 and Cys495
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additional information
the enzyme LP-tan displays alpha/beta structure, featured by a large cap domain inserted into the classical serine hydrolase fold, which is familiar with the feruloyl esterase and lipases. Structure comparisons, overview
additional information
-
the enzyme LP-tan displays alpha/beta structure, featured by a large cap domain inserted into the classical serine hydrolase fold, which is familiar with the feruloyl esterase and lipases. Structure comparisons, overview