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Information on EC 3.1.1.20 - tannase
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3.1.1.20 tannaseIUBMB Comments
Also hydrolyses ester links in other tannins.
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Word Map
- 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
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
tannase, fungal tannase, tannin acyl hydrolase, tanlpl, atan1, tansg1, aotanb, depsidase, tan410, lp-tan, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
tannin acyl hydrolase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
tannin acylhydrolase
Also hydrolyses ester links in other tannins.
CAS REGISTRY NUMBER
COMMENTARY
9025-71-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
epigallocatechin-3-O-(3-O-methyl) gallate + H2O
?
-
-
-
?
epigallocatechin gallate + H2O
gallate + epigallocatechin
-
-
-
?
epigallocatechin gallate + H2O
gallate + epigallocatechin
-
-
-
-
?
additional information
?
-
wild-type enzyme LP-tan has a higher esterase activity than depsidase activity
-
-
?
additional information
?
-
-
wild-type enzyme LP-tan has a higher esterase activity than depsidase activity
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
the enzyme is partially inhibited by but not significantly affected (97.6% residual activity at 1 mM)
phenylmethylsulfonyl fluoride
the enzyme is partially inhibited by but not significantly affected (83.2% residual activity at 1 mM)
Urea
the enzyme is partially inhibited by but not significantly affected (91.4% residual activity at 1 mM)
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
catechin gallate
in 50 mM Tris-HCl (pH 8.0), at 37°C
0.03
epicatechin gallate
in 50 mM Tris-HCl (pH 8.0), at 37°C
0.1
epigallocatechin gallate
in 50 mM Tris-HCl (pH 8.0), at 37°C
0.04
epigallocatechin-3-O-(3-O-methyl) gallate
in 50 mM Tris-HCl (pH 8.0), at 37°C
0.03
gallocatechin gallate
in 50 mM Tris-HCl (pH 8.0), at 37°C
0.62
methyl gallate
wild type enzyme, in 25 mM Tris-HCl (pH 8.0), at 37°C
0.67
methyl gallate
pH 7.0, 37°C, recombinant wild-type enzyme
0.95
methyl gallate
mutant enzyme D421A, in 25 mM Tris-HCl (pH 8.0), at 37°C
1
methyl gallate
mutant enzyme E357A, in 25 mM Tris-HCl (pH 8.0), at 37°C
1.1
methyl gallate
pH 7.0, 37°C, recombinant flap domain-lacking enzyme mutant
1.3
methyl gallate
pH 7.0, 37°C, recombinant mutant P356G
0.53
Tannic acid
pH 7.0, 37°C, recombinant flap domain-lacking enzyme mutant
1.23
Tannic acid
pH 7.0, 37°C, recombinant wild-type enzyme
additional information
additional information
Lineweaver-Burk kinetics
-
additional information
additional information
-
Lineweaver-Burk kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.41
catechin gallate
in 50 mM Tris-HCl (pH 8.0), at 37°C
1.49
epicatechin gallate
in 50 mM Tris-HCl (pH 8.0), at 37°C
1.12
epigallocatechin gallate
in 50 mM Tris-HCl (pH 8.0), at 37°C
0.26
epigallocatechin-3-O-(3-O-methyl) gallate
in 50 mM Tris-HCl (pH 8.0), at 37°C
0.89
gallocatechin gallate
in 50 mM Tris-HCl (pH 8.0), at 37°C
0.53
methyl gallate
mutant enzyme E357A, in 25 mM Tris-HCl (pH 8.0), at 37°C
2.5
methyl gallate
mutant enzyme D421A, in 25 mM Tris-HCl (pH 8.0), at 37°C
46.02
methyl gallate
in 50 mM Tris-HCl (pH 8.0), at 37°C
74
methyl gallate
wild type enzyme, in 25 mM Tris-HCl (pH 8.0), at 37°C
79.8
methyl gallate
pH 7.0, 37°C, recombinant mutant P356G
99.4
methyl gallate
pH 7.0, 37°C, recombinant wild-type enzyme
115.5
methyl gallate
pH 7.0, 37°C, recombinant flap domain-lacking enzyme mutant
62.6
Tannic acid
pH 7.0, 37°C, recombinant wild-type enzyme
69.2
Tannic acid
pH 7.0, 37°C, recombinant flap domain-lacking enzyme mutant
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
53.65
catechin gallate
in 50 mM Tris-HCl (pH 8.0), at 37°C
52.23
epicatechin gallate
in 50 mM Tris-HCl (pH 8.0), at 37°C
11.68
epigallocatechin gallate
in 50 mM Tris-HCl (pH 8.0), at 37°C
6.04
epigallocatechin-3-O-(3-O-methyl) gallate
in 50 mM Tris-HCl (pH 8.0), at 37°C
27.19
gallocatechin gallate
in 50 mM Tris-HCl (pH 8.0), at 37°C
0.021
methyl gallate
mutant enzyme K343A, in 25 mM Tris-HCl (pH 8.0), at 37°C
0.52
methyl gallate
mutant enzyme E357A, in 25 mM Tris-HCl (pH 8.0), at 37°C
2.7
methyl gallate
mutant enzyme D421A, in 25 mM Tris-HCl (pH 8.0), at 37°C
61.4
methyl gallate
pH 7.0, 37°C, recombinant mutant P356G
105
methyl gallate
pH 7.0, 37°C, recombinant flap domain-lacking enzyme mutant
120
methyl gallate
wild type enzyme, in 25 mM Tris-HCl (pH 8.0), at 37°C
148.4
methyl gallate
pH 7.0, 37°C, recombinant wild-type enzyme
50.9
Tannic acid
pH 7.0, 37°C, recombinant wild-type enzyme
130.6
Tannic acid
pH 7.0, 37°C, recombinant flap domain-lacking enzyme mutant
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 10
the enzyme shows more than 80% of activities at a pH range of 8.0-10.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
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
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
50777
1 or 2 * 50777, the tannase exists as both a dimer and a monomer in solution, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer or dimer
1 or 2 * 50777, the tannase exists as both a dimer and a monomer in solution, calculated from amino acid sequence
additional information
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.1 M sodium acetate buffer (pH 5.0) containing 15-20% (w/v) polyethylene glycol 8000 and 0.2 M ammonium sulfate
sitting drop vapor diffusion method, using 14.6% (w/v) PEG 8000 in 0.1 M trisodium citrate pH 5.7
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C204A
the mutant shows about 25% activity compared to the wild type enzyme
D419Ab
the mutant shows less than 5% activity compared to the wild type enzyme
D421A
E357A
H451A
the mutant shows less than 3% activity compared to the wild type enzyme
K343A
the mutant has very little activity compared to the wild type enzyme
K434A
the mutant shows less than 3% activity compared to the wild type enzyme
P356G
site-directed mutagenesis, the mutant P356G only has 48.2% esterase activity compared to wild-type, while it shows a higher depsidase activity (131.7%) than the wild-type enzyme
additional information
D421A
the mutant has 44fold lower activity than the wild type enzyme
D421A
the mutant shows less than 3% activity compared to the wild type enzyme
E357A
the mutant shows less than 5% activity compared to the wild type enzyme
E357A
the mutant has 230fold lower activity than the wild type enzyme
additional information
an enzyme variant lacking the flap-like domain shows reduced esterase (68%) and highly increased depsidase (244%) activity compared to the wild-type enzyme
additional information
-
an enzyme variant lacking the flap-like domain shows reduced esterase (68%) and highly increased depsidase (244%) activity compared to the wild-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45 - 55
the enzyme retains more than 50% activity between 25 and 45°C but the activity drops off markedly above 45°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Q-Sepharose column chromatography, hydroxylapatite column chromatography, and Mono-Q column chromatography
nickel-affinity HisTrap column chromatography and Superdex 200 gel filtration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) and B834(DE3) cells
gene tanLpl, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vaquero, I.; Marcobal, A.; Munoz, R.
Tannase activity by lactic acid bacteria isolated from grape must and wine
Int. J. Food Microbiol.
96
199-204
2004
Lactiplantibacillus plantarum (B3Y018), Lactiplantibacillus plantarum
Iwamoto, K.; Tsuruta, H.; Nishitaini, Y.; Osawa, R.
Identification and cloning of a gene encoding tannase (tannin acylhydrolase) from Lactobacillus plantarum ATCC 14917(T)
Syst. Appl. Microbiol.
31
269-277
2008
Lactiplantibacillus plantarum (B3Y018), Lactiplantibacillus plantarum
Wu, M.; Peng, X.; Wen, H.; Wang, Q.; Chen, Q.; McKinstry, W.J.; Ren, B.
Expression, purification, crystallization and preliminary X-ray analysis of tannase from Lactobacillus plantarum
Acta Crystallogr. Sect. F
69
456-459
2013
Lactiplantibacillus plantarum (B3Y018), Lactiplantibacillus plantarum
Ueda, S.; Nomoto, R.; Yoshida, K.; Osawa, R.
Comparison of three tannases cloned from closely related Lactobacillus species: L. plantarum, L. paraplantarum, and L. pentosus
BMC Microbiol.
14
87
2014
Lactiplantibacillus pentosus, Lactiplantibacillus paraplantarum, Lactiplantibacillus plantarum (B3Y018), Lactiplantibacillus plantarum, Lactiplantibacillus pentosus 21A-3, Lactiplantibacillus paraplantarum NSO120, Lactiplantibacillus plantarum ATCC 14917T (B3Y018)
Ren, B.; Wu, M.; Wang, Q.; Peng, X.; Wen, H.; McKinstry, W.J.; Chen, Q.
Crystal structure of tannase from Lactobacillus plantarum
J. Mol. Biol.
425
2737-2751
2013
Lactiplantibacillus plantarum (B3Y018), Lactiplantibacillus plantarum
Matoba, Y.; Tanaka, N.; Noda, M.; Higashikawa, F.; Kumagai, T.; Sugiyama, M.
Crystallographic and mutational analyses of tannase from Lactobacillus plantarum
Proteins
81
2052-2058
2013
Lactiplantibacillus plantarum (B3Y018), Lactiplantibacillus plantarum, Lactiplantibacillus plantarum SN35N (B3Y018)
Wang, D.; Liu, Y.; Lv, D.; Hu, X.; Zhong, Q.; Zhao, Y.; Wu, M.
Substrates specificity of tannase from Streptomyces sviceus and Lactobacillus plantarum
AMB Express
8
147
2018
Streptomyces sviceus (A0A077YGC3), Streptomyces sviceus, Lactiplantibacillus plantarum (B3Y018), Lactiplantibacillus plantarum
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