Information on EC 4.2.2.12 - xanthan lyase

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The enzyme appears in viruses and cellular organisms

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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-
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SYSTEMATIC NAME
IUBMB Comments
xanthan lyase
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CAS REGISTRY NUMBER
COMMENTARY hide
113573-69-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
enzyme is induced by xanthan
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Manually annotated by BRENDA team
enzyme is induced by xanthan
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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
pyruvylated xanthan
pyruvylate mannose + xanthan oligosaccharides
show the reaction diagram
xanthan
D-xylooligosaccharides
show the reaction diagram
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-
-
-
?
xanthan
oligosaccharide
show the reaction diagram
xanthan
oligosaccharides
show the reaction diagram
xanthan
pyruvylate mannose + oligosaccharide
show the reaction diagram
additional information
?
-
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no substrate: p-nitrophenyl-beta-D-mannose, unsubstituted terminal beta-D-mannose residues of xanthan
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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
xanthan
oligosaccharide
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
10 mM, 194% of initial activity
Co2+
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1 mM, slight stimulation
K+
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10 mM, 196% of initial activity
Li+
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10 mM, 192% of initial activity
Mg2+
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10 mM, 187% of initial activity
Mn2+
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10 mM, 152% of initial activity
Na+
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10 mM, 192% of initial activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4,6-O-[(1S)-1-carboxyethylidene]-beta-D-mannopyranose
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Cu2+
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10 mM, 19% residual activity
CuCl2
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0.1 mM, 70% loss of activity
D-mannose
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HgCl2
iodoacetamide
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1 mM, 70% loss of activity
Zn2+
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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
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30°C, pH 6.9
28.2
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pH 6.0, 40°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
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plus 0.05 M NaCl
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.7
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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
UNIPROT
ORGANISM
Bacillus sp. (strain GL1);
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
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gel filtration
75000
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gel filtration
85000
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x * 85000, SDS-PAGE
100000
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x * 100000, SDS-PAGE, deduced from gene sequence: enzyme has a 36 amino acid signal sequence, mature enzyme has 97000 Da
110000
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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
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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
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purification from culture liquid
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is induced by xanthan
expression is inhibited by glucose
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H246A
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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
H246A
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mutant with 2fold decreased Km for xanthan, 500fold decreased turnover number
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N194A
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mutant with 2fold decreased Km for xanthan, 570fold decreased turnover number
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Y255F
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mutant with 2fold decreased Km for xanthan, 360fold decreased turnover number
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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
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KM-value for xanthan is 1.8fold higher than wild type value. kcat for xanthan is 1.3fold lower than wild-type value