Information on EC 3.2.1.131 - xylan alpha-1,2-glucuronosidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.2.1.131
-
RECOMMENDED NAME
GeneOntology No.
xylan alpha-1,2-glucuronosidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of (1->2)-alpha-D-(4-O-methyl)glucuronosyl links in the main chain of hardwood xylans
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
xylan 2-alpha-D-(4-O-methyl)glucuronohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
114921-73-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
307
-
-
Manually annotated by BRENDA team
307
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cf. EC 3.2.1.131
UniProt
Manually annotated by BRENDA team
cf. EC 3.2.1.131
UniProt
Manually annotated by BRENDA team
growth on wheat bran
-
-
Manually annotated by BRENDA team
Polyporus versicolor
-
-
-
Manually annotated by BRENDA team
No.3; No.4; No.5
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-
Manually annotated by BRENDA team
No.3
-
-
Manually annotated by BRENDA team
No.4
-
-
Manually annotated by BRENDA team
No.5
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Tyromyces palustris
highest active producer among Trichoderma and 5 basidomycete species
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-O-methyl-beta-D-glucopyranuronosyl-(1->2)-[beta-D-xylopyranosyl-(1->4)]-beta-D-xylopyranosyl-(1->4)-D-xylopyranose + H2O
3-O-methyl-alpha-D-glucuronic acid + beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylopyranose
show the reaction diagram
4-deoxy-beta-L-threo-hex-4-enopyranosyl-(1->2)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranose + H2O
4-deoxy-beta-L-threo-hex-4-enopyranose + beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranose
show the reaction diagram
-
-
-
ir
4-O-Me-GlcA-alpha-(1->2)-Xyl-beta(1->4)-Xyl + H2O
?
show the reaction diagram
4-O-methyl-alpha-D-glucopyranosyl-(1->2)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranose + H2O
4-O-methyl-alpha-D-glucopyranose + 4-O-beta-D-xylopyranosyl-beta-D-xylopyranose
show the reaction diagram
aldobiouronic acid + H2O
4-O-methyl-alpha-D-glucuronic acid
show the reaction diagram
-
-
-
-
?
aldobiouronic acid + H2O
D-xylose + 4-O-methyl-D-glucuronic acid
show the reaction diagram
aldobiuronic acid + H2O
D-xylose + ?
show the reaction diagram
aldopentaouronic acid + H2O
4-O-methyl-alpha-D-glucuronic acid
show the reaction diagram
-
-
-
-
?
aldopentaouronic acid + H2O
4-O-methyl-D-glucuronic acid + Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xyl
show the reaction diagram
-
-
-
?
aldopentaouronic acid + H2O
4-O-methyl-glucuronic acid + Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xyl
show the reaction diagram
aldotetraouronic acid + H2O
4-O-methyl-alpha-D-glucuronic acid
show the reaction diagram
aldotetraouronic acid + H2O
4-O-methyl-D-glucuronic acid + Xylbeta(1-4)Xylbeta(1-4)Xyl
show the reaction diagram
-
-
-
?
aldotetraouronic acid + H2O
4-O-methyl-glucuronic acid + Xylbeta(1-4)Xylbeta(1-4)Xyl
show the reaction diagram
aldotriouronic acid + H2O
4-O-methyl-alpha-D-glucuronic acid
show the reaction diagram
-
-
-
-
?
aldotriouronic acid + H2O
4-O-methyl-glucuronic acid + 4-O-beta-D-xylosyl-D-xylose
show the reaction diagram
aldouronic acid + H2O
?
show the reaction diagram
beech glucuronoxylan + H2O
4-O-methyl-D-glucuronic acid + ?
show the reaction diagram
-
-
-
?
beechwood xylan + H2O
4-O-methyl-alpha-D-glucuronic acid + ?
show the reaction diagram
beechwood xylan + H2O
4-O-methyl-alpha-D-glucuronic acid + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
beechwood xylan + H2O
4-O-methyl-alpha-D-glucuronic acid + glucuronic acid
show the reaction diagram
birchwood xylan + H2O
4-O-methyl-alpha-D-glucuronic acid + ?
show the reaction diagram
-
-
-
?
birchwood xylan + H2O
4-O-methyl-alpha-D-glucuronic acid + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
birchwood xylan + H2O
4-O-methyl-alpha-D-glucuronic acid + glucuronic acid
show the reaction diagram
birchwood xylan + H2O
4-O-methyl-D-glucuronic acid + D-glucuronic acid + ?
show the reaction diagram
-
-
-
?
birchwood xylan oligosaccharides + H2O
?
show the reaction diagram
glucuronoxylan + H2O
4-O-methyl-alpha-D-glucuronic acid + ?
show the reaction diagram
glucuronoxylan alpha-(4-O-methyl)-glucuronide + H2O
xylotriose + xylotetraose + ?
show the reaction diagram
oat spelt xylan + H2O
4-O-methyl-D-glucuronic acid + D-glucuronic acid + ?
show the reaction diagram
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1% of the activity with birchwood xylan
-
?
spruce arabinoxylan + H2O
4-O-methyl-D-glucuronic acid + D-glucuronic acid + ?
show the reaction diagram
-
37% of the activity with birchwood xylan
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?
Xyl-beta-(1->4)-[4-O-Me-GlcA-alpha-(1->2)]-Xyl-beta(1->4)-Xyl + H2O
?
show the reaction diagram
-
-
-
-
?
Xyl-Xyl(MeGlcA)-Xyl-Xyl + H2O
4-O-methyl-alpha-D-glucuronic acid + xylotetraose
show the reaction diagram
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-
-
-
?
xylan + H2O
4-O-methyl-alpha-D-glucuronic acid + ?
show the reaction diagram
xylan + H2O
xylobiose
show the reaction diagram
-
-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
aldouronic acid + H2O
?
show the reaction diagram
beechwood xylan + H2O
4-O-methyl-alpha-D-glucuronic acid + ?
show the reaction diagram
beechwood xylan + H2O
4-O-methyl-alpha-D-glucuronic acid + glucuronic acid
show the reaction diagram
birchwood xylan + H2O
4-O-methyl-alpha-D-glucuronic acid + ?
show the reaction diagram
I2E7L0
-
-
-
?
birchwood xylan + H2O
4-O-methyl-alpha-D-glucuronic acid + glucuronic acid
show the reaction diagram
xylan + H2O
4-O-methyl-alpha-D-glucuronic acid + ?
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
the presence of manganese produces higher activity (117.4%)
additional information
enzyme activity is not dramatically impacted by Co2+, Cu2+, Fe2+, Li+, Mg2+, and Zn2+ at 1 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
Ca2+ addition results in a slight activity decrease (86.3%)
Cd2+
1 mM, 40% residual activity
additional information
not inhibitory: EDTA at 10 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
xylanase
when the enzyme is used in combination with xylanase, a large stimulation in activity occurs
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19.5
4-O-Me-GlcA-alpha-(1->2)-Xyl-beta(1->4)-Xyl
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in 50 mM sodium phosphate, 12 mM citrate buffer, pH 6.5, at 37C
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3
4-O-methyl-alpha-D-glucopyranosyl-(1->2)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranose
pH 6.5, 80C
0.53
aldobiouronic acid
-
37C, pH 6.5
0.42
aldopentaouronic acid
-
37C, pH 6.5
0.2 - 0.36
aldotetraouronic acid
0.28
aldotriouronic acid
-
37C, pH 6.5
0.4
beechwood xylan
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in 50 mM sodium phosphate, 12 mM citrate buffer, pH 6.5, at 37C
-
0.3
birchwood xylan
-
in 50 mM sodium phosphate, 12 mM citrate buffer, pH 6.5, at 37C
-
4.5
Xyl-beta-(1->4)-[4-O-Me-GlcA-alpha-(1->2)]-Xyl-beta(1->4)-Xyl
-
in 50 mM sodium phosphate, 12 mM citrate buffer, pH 6.5, at 37C
-
additional information
birchwood xylan
km value of wild-type 43 mg/ml, pH 6.5, 40C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
18.4
4-O-Me-GlcA-alpha-(1->2)-Xyl-beta(1->4)-Xyl
Bacteroides ovatus
-
in 50 mM sodium phosphate, 12 mM citrate buffer, pH 6.5, at 37C
-
117
4-O-methyl-alpha-D-glucopyranosyl-(1->2)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranose
Pseudothermotoga thermarum
F7YUS1
pH 6.5, 80C
69.2
aldobiouronic acid
Cellvibrio japonicus
-
37C, pH 6.5
132
aldopentaouronic acid
Cellvibrio japonicus
-
37C, pH 6.5
54.9 - 103
aldotetraouronic acid
96
aldotriouronic acid
Cellvibrio japonicus
-
37C, pH 6.5
1082
aldouronic acid
Paenibacillus curdlanolyticus
A0A0A0V7L5
pH 6.0, 40C
-
11.6
beechwood xylan
Bacteroides ovatus
-
in 50 mM sodium phosphate, 12 mM citrate buffer, pH 6.5, at 37C
-
0.008 - 289
birchwood xylan
-
53.9
Xyl-beta-(1->4)-[4-O-Me-GlcA-alpha-(1->2)]-Xyl-beta(1->4)-Xyl
Bacteroides ovatus
-
in 50 mM sodium phosphate, 12 mM citrate buffer, pH 6.5, at 37C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
4-O-Me-GlcA-alpha-(1->2)-Xyl-beta(1->4)-Xyl
Bacteroides ovatus
-
in 50 mM sodium phosphate, 12 mM citrate buffer, pH 6.5, at 37C
202171
29
beechwood xylan
Bacteroides ovatus
-
in 50 mM sodium phosphate, 12 mM citrate buffer, pH 6.5, at 37C
11539
37
birchwood xylan
Bacteroides ovatus
-
in 50 mM sodium phosphate, 12 mM citrate buffer, pH 6.5, at 37C
1733
12
Xyl-beta-(1->4)-[4-O-Me-GlcA-alpha-(1->2)]-Xyl-beta(1->4)-Xyl
Bacteroides ovatus
-
in 50 mM sodium phosphate, 12 mM citrate buffer, pH 6.5, at 37C
202170
additional information
birchwood xylan
Saccharophagus degradans
Q21JW4
kcat/Km value of wild-type 6.7 ml/s/ml, pH 6.5, 40C
1733
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.67
concentrated induction medium
6.2
9.2fold purified enzyme
42
-
after gel filtration
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 5.5
at pH 4.0 and pH 5.5 the activities represent 25.5% and 51.6% of the activity at the optimum pH, respectively
4.5 - 7.5
-
at pH 4.5 and 7.5 retains 40% of enzyme activity
5 - 8
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more than 50% activity between pH 5.0 and 8.0
6 - 9
there is a dramatic decrease in enzyme activity at pH 6.0 and pH 9.0, and there is little activity at pH 4.0 and pH 5.0
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 90
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more than 60% activity between 40 and 90C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.6
-
isoelectric focusing
4.4
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isoelectric focusing
4.5
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
77000
-
alpha2, 2 * 77000, SDS-PAGE, crystal structure
78480
-
alpha2, 2 * 78480, deduced from nucleotide sequence
80000
-
2 * 80000, SDS-PAGE
80343
-
2 * 80343, calculated from amino acid sequence
84500
x * 84500, calculated from amino acid sequence
85000
-
2 * 85000, calculated from amino acid sequence
91725
-
2 * 91725, calculated from amino acid sequence
100000
-
x * 100000, SDS-PAGE
107000
x * 107000, mature protein, calculated from amino acid sequence
110000
-
gel filtration
120000
x * 120000, SDS-PAGE
125000
-
x * 125000, SDS-PAGE
150000
163700
-
gel filtration
189000
sedimentation-equilibrium ultracentrifugation
199000
-
analytical ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using 19% (w/v) PEG3350, 0.2 M sodium citrate, pH 5.5
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vapor phase diffusion using the hanging drop method, 250 mM MgCl2 and 20% v/v ethylene glycol with 15% w/v polyethylene glycol 3350 as prcipitant at 20C, triclinic space group P1 with a: 69.9 A, b: 74.7 A, c: 87.6 A, alpha: 115.2, beta: 93.1 and gamma: 109.3
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hanging drop method at 20C, 10 mg/ml enzyme solution mixed with an equal volume of reservoir solution, containing 14% w/v polyethylene glycol 4000, 12% v/v isopropyl alcohol and 0.1 M sodium citrate, pH 5.5, tetragonal space group P41212 with a and b: 74.6 A and c: 330.3 A
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two crystal forms, form T1 is obtained by the vapour-diffusion method using polyethylene glycol as precipitant and 2-propanol as organic additive, tetragonal space group P41212 or P43212 with a and b: 76.1 A and c: 331.2 A, form M1 at slightly lower pH and lower concentration of 2-propanol, monoclinic space group P21 with a: 65.8 A, b: 127.4 A, c: 96.6 A and beta: 97.9
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structural analysis. Residue E288 acts at the catalytic proton donor, D367 and E395 are likely nucleophilic bases
structure reveals a five-domain architecture, with an additional insertion C+ domain that has significant impact on the domain arrangement of the protein monomer and its dimerization. The participation of domain C+ in substrate binding is supported by reduced substrate inhibition upon introducing W773A, W689A, and F696A substitutions within this domain. In addition to Asp335, residue Glu216 is essential for the catalytic activtiy
sitting drop vapor diffusion method, using 16% (w/v) PEG 2000 MME and 0.1 M Tris pH 7.0
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
stable for prolonged times
666694
5.5 - 9.5
4C, 24 h, more than 50% residual activity
738687
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
half-life 90 min
40 - 60
after 2 h at 40 and 50C, the enzyme retains most of the initial activity. At 60 C, half of the activity is lost at 30 min, and no activity remains after 1 h
65
2 h, 98% residual activity
73.4
-
denaturation temperature
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
labile even if frozen
Tyromyces palustris
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HisTrap HP column chromatography
immobilized metal affinity chromatography and Superdex 75 gel filtration
-
Ni-affinity column chromatography and Superdex 200 gel filtration
-
Ni-NTA column chromatography, and gel filtration
-
purified from a concentrated induction medium (mixture of xylobiose, xylotriose and methyl beta-D-xylopyranoside) by a combination of ion-exchange and hydrophobic interaction chromatographies, 9.2fold
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)pLysE cells
expressed in Escherichia coli SOLR cells carrying pBS expression vectors encoding the alpha-glucuronidase gene
-
expressed in Pichia pastoris strain GS115
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expression as a His10-thioredoxin fusion protein in Escherichia coli
-
expression in Escherichia coli
overexpression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
alpha-glucuronidase agu1 is not expressed on glucose and xylose
low expression of alpha-glucuronidase agu1 is observed on glucuronic acid
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D192A
-
the mutant shows wild type activity
D206A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
D332A
-
inactive
D396N
-
the mutant shows strongly reduced activity compared to the wild type enzyme
D478A
-
the mutant shows wild type activity
E162A
-
the mutant shows wild type activity
E375A
-
almost inactive
E782A
-
the mutant shows reduced activity compared to the wild type enzyme
E785A
-
the mutant shows reduced activity compared to the wild type enzyme
H275A
-
the mutant shows severely reduced activity compared to the wild type enzyme
H275A/H422A
-
inactive
H422A
-
almost inactive
K374A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
N205A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
N398A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
N462A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
R328A
-
almost inactive
W169A
-
the mutant shows wild type activity
W249A
-
the mutant shows severely reduced activity compared to the wild type enzyme
Y373A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
Y420A
-
the mutant shows severely reduced activity compared to the wild type enzyme
Y425A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
Y788A
-
the mutant shows reduced activity compared to the wild type enzyme
Y792A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
D192A
-
the mutant shows wild type activity
-
D206A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
-
D332A
-
inactive
-
W169A
-
the mutant shows wild type activity
-
Y420A
-
the mutant shows severely reduced activity compared to the wild type enzyme
-
D365A
-
much less active than wild type
D365C
-
much less active than wild type
E292A
-
much less active than wild type
E292C
-
much less active than wild type
E393A
-
much less active than wild type
E393C
-
less active than wild type
AguADELTAC
-
lacks the last 81 amino acids, heat labile, 0.1% of the specific activity of the wild-type enzyme at 35C
AguADELTAN
-
lacks the first 126 amino acids, 1% of the specific activity of the wild-type enzyme at 55C
AguADELTANC
-
lacks the first 126 and last 81 amino acids, is insoluble
D274A
-
no change in activity
D364A
-
great decrease in activity
E158N
-
decrease in activity
E285N
-
decrease in activity
E386Q
-
decrease in activity
E392C
-
great decrease in activity
E510A
-
decrease in activity
D215A
15fold decrease in catalytic efficiency
D335A
complete loss of activtiy; weak binding of substrate
E216A
complete loss of activtiy
E381A
330fold decrease in catalytic efficiency
F696A
3-5fold decrease in kcat value
R331A
26000fold decrease in catalytic efficiency
W689A
3-5fold decrease in kcat value
W773A
3-5fold decrease in kcat value
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
additional information
Show AA Sequence (649 entries)
Please use the Sequence Search for a specific query.