Information on EC 4.2.2.25 - gellan lyase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.2.2.25
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RECOMMENDED NAME
GeneOntology No.
gellan lyase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Eliminative cleavage of beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyluronate bonds of gellan backbone releasing tetrasaccharides containing a 4-deoxy-4,5-unsaturated D-glucopyranosyluronic acid at the non-reducing end. The tetrasaccharide produced from deacetylated gellan is beta-D-4-deoxy-Delta4-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp.
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
gellan degradation
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SYSTEMATIC NAME
IUBMB Comments
gellan beta-D-glucopyranosyl-(1->4)-D-glucopyranosyluronate lyase
The enzyme is highly specific to gellan, especially deacetylated gellan.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain GL1
SwissProt
Manually annotated by BRENDA team
soil microorganism, microbial strain for lyase production not specified
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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
gellan
?
show the reaction diagram
[beta-D-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp-(1->4)-beta-D-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp-(1->4)-]n
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp + [beta-D-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp-(1->4)-beta-D-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp-(1->4)-]n-1
show the reaction diagram
i.e. deacetylated gellan. The purified gellan lyase depolymerizes deacetylated gellan and gives a single oligosaccharide product with a molecular weight of 646 Da, which is determined by fast atom bombardment mass spectrometry. The structure of the product is determined by the combination of mass spectrometry, HPLC analysis, and high-resolution proton nuclear magnetic resonance spectroscopy to be a tetrasaccharide of glucuronyl-glucosyl-rhamnosyl-glucose with unsaturated glucuronic acid at the nonreducing terminal
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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
gellan
?
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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Ca2+, Co2+, Cu2+, Fe2+, Mo2+, Mg2+, and Zn2+ show no effect on the enzyme activity at 1 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
1 mM, 50% inhibition
N-bromosuccinimide
1 mM, 81% inhibition
p-chloromercuribenzoate
1 mM, 39% inhibition
sodium lauryl sulfate
1 mM, 81% inhibition
Urea
1 mM, 22% inhibition
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CaCl2
1 mM, 1.4fold activation
FeCl2
1 mM, 1.2fold activation
KCl
1 mM, 1.4fold activation
Li2SO4
1 mM, 1.3fold activation
MgCl2
1 mM, 1.4fold activation
MnCl2
1 mM, 1.4fold activation
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.671
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pH 7.0, 30C
9.34
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pH 7.0, 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
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pH 5.0: about 35% of maximal activity, pH 9.0: about 50% of maximal activity
5 - 10
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pH 5.0: about 40% of maximal activity, pH 10.0: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 60
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30C: about 75% of maximal activity, 60C: about 40% of maximal activity
30 - 50
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30C: about 45% of maximal activity, 50C: 50% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
3 * or 4 * 120000, SDS-PAGE
140000
216000
capillary gel electrophoresis
220000
x * 220000, SDS-PAGE
250000
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gel filtration
259456
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1 * 259456, calculated from sequence
260000
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1 * 260000, SDS-PAGE
350000
two protein bands are observed: 350000 Da and 480000 Da, non-denaturing gel electrophoresis
480000
two protein bands are observed: 350000 Da and 480000 Da, non-denaturing gel electrophoresis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method at 18C
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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pH 7.5, 10 min, 50% loss of activity
55
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pH 7.0, 10 min, more than 50% loss of activity
70
half-life: 50 min in absence of substrate. Stable for 2.5 h in presence of substrate
75
at pH 7.2 and a protein concentration above 1 mg/ml large exothermic aggregation occurrs near Tm (75C) rendering that the unfolding transition is irreversible
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
microbial strain for lyase production not specified
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme activity increases tenfold in conditions of continuous cultivation compared to data from batch fermentations and enzyme productivity is almost sixfold higher
indicible in presence of gellan
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the enzyme is consitutively produced. Gellan lyase is efficiently induced in presence of xanthan
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