Information on EC 4.2.2.12 - xanthan lyase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
4.2.2.12
-
RECOMMENDED NAME
GeneOntology No.
xanthan lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Eliminative cleavage of the terminal beta-D-mannosyl-(1->4)-beta-D-glucuronosyl linkage of the side-chain of the polysaccharide xanthan, leaving a 4-deoxy-alpha-L-threo-hex-4-enuronosyl group at the terminus of the side-chain
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-elimination
-
-
elimination of an alcohol from a polysaccharide
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
xanthan lyase
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CAS REGISTRY NUMBER
COMMENTARY hide
113573-69-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
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Manually annotated by BRENDA team
strain XL-1, enzyme is induced by xanthan
-
-
Manually annotated by BRENDA team
strain XL-1, enzyme is induced by xanthan
-
-
Manually annotated by BRENDA team
heat-stable, salt-tolerant mixed culture NRRL B-14401
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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
pyruvylated xanthan
pyruvylate mannose + oligosaccharides
show the reaction diagram
-
best substrate
-
?
pyruvylated xanthan
pyruvylate mannose + xanthan oligosaccharides
show the reaction diagram
xanthan
D-xylooligosaccharides
show the reaction diagram
-
-
-
-
?
xanthan
oligosaccharide
show the reaction diagram
xanthan
oligosaccharides
show the reaction diagram
xanthan
pyruvylate mannose + oligosaccharide
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
no substrate: p-nitrophenyl-beta-D-mannose, unsubstituted terminal beta-D-mannose residues of xanthan
-
-
-
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
xanthan
oligosaccharide
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
10 mM, 194% of initial activity
Co2+
-
1 mM, slight stimulation
K+
-
10 mM, 196% of initial activity
Li+
-
10 mM, 192% of initial activity
Mg2+
-
10 mM, 187% of initial activity
Mn2+
-
10 mM, 152% of initial activity
Na+
-
10 mM, 192% of initial activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4,6-O-[(1S)-1-carboxyethylidene]-beta-D-mannopyranose
-
-
Cu2+
-
10 mM, 19% residual activity
CuCl2
-
0.1 mM, 70% loss of activity
D-mannose
-
-
iodoacetamide
-
1 mM, 70% loss of activity
Zn2+
-
10 mM, 53% residual activity
additional information
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not inhibitory: CoCl2, MgCl2, CaCl2 at 1 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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1 mM, slight stimulation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
Xanthan
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0.25 mg/ml, wild-type
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.92 - 6120
Xanthan
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.21 - 19.2
4,6-O-[(1S)-1-carboxyethylidene]-beta-D-mannopyranose
4 - 837
D-mannose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.62
-
30C, pH 6.9
6.28
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pH 7.0
28.2
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pH 6.0, 40C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
plus 0.05 M NaCl
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
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at 4C
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.7
-
isoelectric focusing
7.9
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus sp. (strain GL1)
Bacillus sp. (strain GL1)
Bacillus sp. (strain GL1)
Bacillus sp. (strain GL1)
Bacillus sp. (strain GL1)
Bacillus sp. (strain GL1)
Bacillus sp. (strain GL1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
-
gel filtration
75000
-
gel filtration
110000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion, resolution of N194A/PyrMan, N194/pentasacharide and ligand-free form are 1.8, 2.1 and 2.3 respectively
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structure of wild-type enzyme, wild type enzyme in complex with ryruvated D-mannose and mutant enzyme R612A, hanging-drop vapor diffusion
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
20 mM sodium phosphate, pH 5.0, 0.25 M NaCl, stable for 6h
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in Escherichia coli
-
partial
-
purification from culture liquid
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is induced by xanthan
expression is inhibited by glucose
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H246A
-
mutant with 2fold decreased Km for xanthan, 500fold decreased turnover number
N194A
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mutant with 2fold decreased Km for xanthan, 570fold decreased turnover number
Y255F
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mutant with 2fold decreased Km for xanthan, 360fold decreased turnover number
R313A
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KM-value for xanthan is 1.5fold higher than wild type value. kcat for xanthan is 219fold lower than wild-type value
R612A
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KM-value for xanthan is 11.6fold higher than wild type value. kcat for xanthan is 2.8fold higher than wild-type value
Y315F
-
KM-value for xanthan is 1.8fold higher than wild type value. kcat for xanthan is 1.3fold lower than wild-type value