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

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UNIPROT: Q21JW4 not found.
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
axyagu115a, agu67a, btgh115a, scagu115, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-(1->2)-glucuronidase
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glucuronidase, 1,2-alpha-
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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SYSTEMATIC NAME
IUBMB Comments
xylan 2-alpha-D-(4-O-methyl)glucuronohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
114921-73-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
birchwood xylan + H2O
4-O-methyl-D-glucuronic acid + D-glucuronic acid + ?
show the reaction diagram
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-
-
?
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
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?
spruce arabinoxylan + H2O
4-O-methyl-D-glucuronic acid + D-glucuronic acid + ?
show the reaction diagram
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37% of the activity with birchwood xylan
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?
additional information
?
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the enzyme shows activity toward glucuronoxylan and oligomers thereof with preference toward 4-O-methyl glucopyranosyluronic acid linked to internal xylopyranosyl residues
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
1 mM, 30% residual activity
Cd2+
1 mM, 40% residual activity
Cu2+
1 mM, no residual activity
Hg2+
1 mM, no residual activity
Ni2+
1 mM, 70% residual activity
Zn2+
1 mM, 10% residual activity
additional information
not inhibitory: EDTA at 10 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
birchwood xylan
km value of wild-type 43 mg/ml, pH 6.5, 40°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.008 - 289
birchwood xylan
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
birchwood xylan
kcat/Km value of wild-type 6.7 ml/s/ml, pH 6.5, 40°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q21JW4_SACD2
Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024)
975
0
109992
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70800
sedimentation-equilibrium ultracentrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 109992, calculated
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D215A
15fold decrease in catalytic efficiency
D335A
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9.5
4°C, 24 h, more than 50% residual activity
738687
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
half-life 90 min
40
half-life 60 min
70
2 min, complete loss of activtiy
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, W.; Yan, R.; Nocek, B.P.; Vuong, T.V.; Di Leo, R.; Xu, X.; Cui, H.; Gatenholm, P.; Toriz, G.; Tenkanen, M.; Savchenko, A.; Master, E.R.
Biochemical and structural characterization of a five-domain GH115 alpha-Glucuronidase from the marine bacterium Saccharophagus degradans 2-40T
J. Biol. Chem.
291
14120-14133
2016
Saccharophagus degradans (Q21JW4), Saccharophagus degradans DSM 17024 (Q21JW4)
Manually annotated by BRENDA team