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
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gallic
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tannic
- aspergillus
- niger
- gallate
- plantarum
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submerged
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solid-state
- food industry
- catechin
- pectinase
- biotechnology
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tannery
- 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
- 1-propanol
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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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General Information
General Information on EC 3.1.1.20 - tannase
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physiological function
additional information
enzyme titre with the recombinant strain (390 U/l) is approximately 10times higher than that in the control strain without the TEF1 promoter-ATAN1 gene expression cassette. The Atan1 protein contains at positions 210-214 the canonical Gly-X-Ser-X-Gly motif found in the serine hydrolases as the catalytic triad for nucleophilic serine
physiological function
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tanA gene is specific to Staphylococcus lugdunensis
physiological function
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the enzyme production follows logarithmic growth phase with maximum enzyme yield being obtained after 6 days corresponding to the culture pH of 3.8
physiological function
tannase and the organism itself are employed to protect grazing animals and environment against the toxic effects caused by tannins in them
physiological function
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one of the most important functions of tannic acid hydrolase is the release of gallic acid (GA) from complex tannins
physiological function
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one of the most important functions of tannic acid hydrolase is the release of gallic acid (GA) from complex tannins
physiological function
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one of the most important functions of tannic acid hydrolase is the release of gallic acid (GA) from complex tannins
physiological function
tannase catalyses the breakdown of ester and depside link-ages in hydrolysable tannins such as tannic acid, producing gallic acid and glucose
physiological function
tannases can catalyze the hydrolysis of galloyl ester and depside bonds of hydrolysable tannins to release gallic acid and glucose, but tannases from different species have different substrate specificities. The enzymes can also show depsidase activity
physiological function
tannases can catalyze the hydrolysis of galloyl ester and depside bonds of hydrolysable tannins to release gallic acid and glucose, but tannases from different species have different substrate specificities. The enzymes can also show depsidase activity
physiological function
tannin acyl hydrolases, or tannases, catalyze the hydrolysis of ester bonds in gallotannins, complex tannins, and gallic acid esters, usually with gallic acid as the main product
physiological function
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the inducible, largely extracellular enzyme causes the hydrolysis of ester and depside bonds present in various substrates
physiological function
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the inducible, largely extracellular enzyme causes the hydrolysis of ester and depside bonds present in various substrates
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physiological function
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tannin acyl hydrolases, or tannases, catalyze the hydrolysis of ester bonds in gallotannins, complex tannins, and gallic acid esters, usually with gallic acid as the main product
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physiological function
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enzyme titre with the recombinant strain (390 U/l) is approximately 10times higher than that in the control strain without the TEF1 promoter-ATAN1 gene expression cassette. The Atan1 protein contains at positions 210-214 the canonical Gly-X-Ser-X-Gly motif found in the serine hydrolases as the catalytic triad for nucleophilic serine
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physiological function
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tannase and the organism itself are employed to protect grazing animals and environment against the toxic effects caused by tannins in them
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physiological function
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tannase catalyses the breakdown of ester and depside link-ages in hydrolysable tannins such as tannic acid, producing gallic acid and glucose
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physiological function
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tannase catalyses the breakdown of ester and depside link-ages in hydrolysable tannins such as tannic acid, producing gallic acid and glucose
-
physiological function
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the enzyme production follows logarithmic growth phase with maximum enzyme yield being obtained after 6 days corresponding to the culture pH of 3.8
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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
additional information
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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
additional information
the enzyme LP-tan forms a flap domain (amino acids 225-247) and a sandwich structure (Ile206-substrate-Pro356), functional role of sandwich structure and the flap (flap-like) domain in the substrate specificity of tannase, overview. The sandwich and the flap domain can help in catalytic hydrolysis of ester bonds
additional information
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the enzyme LP-tan forms a flap domain (amino acids 225-247) and a sandwich structure (Ile206-substrate-Pro356), functional role of sandwich structure and the flap (flap-like) domain in the substrate specificity of tannase, overview. The sandwich and the flap domain can help in catalytic hydrolysis of ester bonds
additional information
the enzyme SS-tan forms a sandwich structure (Ile253-substrate-Gly384), but no flap domain, it forms a flap-like domain (amino acids: 93-143) instead, functional role of sandwich structure and the flap (flap-like) domain in the substrate specificity of tannase, overview. The sandwich and the flap domain can help in catalytic hydrolysis of ester bonds, while the flap-like domain in SS-tan mainly works on depside bonds
additional information
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the enzyme SS-tan forms a sandwich structure (Ile253-substrate-Gly384), but no flap domain, it forms a flap-like domain (amino acids: 93-143) instead, functional role of sandwich structure and the flap (flap-like) domain in the substrate specificity of tannase, overview. The sandwich and the flap domain can help in catalytic hydrolysis of ester bonds, while the flap-like domain in SS-tan mainly works on depside bonds
additional information
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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
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additional information
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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
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