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Information on EC 4.2.2.25 - gellan lyase and Organism(s) Geobacillus stearothermophilus and UniProt Accession P85513

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.2 Acting on polysaccharides
                4.2.2.25 gellan lyase
IUBMB Comments
The enzyme is highly specific to gellan, especially deacetylated gellan.
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This record set is specific for:
Geobacillus stearothermophilus
UNIPROT: P85513
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Word Map
The taxonomic range for the selected organisms is: Geobacillus stearothermophilus
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Reaction Schemes
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.
Synonyms
gellan lyase, more
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
gellan beta-D-glucopyranosyl-(1->4)-D-glucopyranosyluronate lyase
The enzyme is highly specific to gellan, especially deacetylated gellan.
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
NATURAL SUBSTRATE
NATURAL 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
gellan lyase cleaves the gellan molecule to tetrasaccharide-repeating units of glucuronic acid-glucose-rhamnose-glucose through the reaction of beta-elimination. Gellan is depolymerized first by gellan lyase and the received tetrasaccharide further hydrolyzed by certain exoenzymes which are found outside the cell in the stationary phase
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
1 mM, 50% inhibition
EDTA
1 mM, 22% 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
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the strain produces thermostable gellan lyase extracellularly during exponential phase
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Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GELL_GEOSE
204
0
20542
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
3 * or 4 * 120000, SDS-PAGE
216000
capillary gel electrophoresis
220000
x * 220000, 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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method at 18°C
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 (75°C) rendering that the unfolding transition is irreversible
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Derekova, A.; Sjholm, C.; Mandeva, R.; Michailova, L.; Kambourova, M.
Biosynthesis of a thermostable gellan lyase by newly isolated and characterized strain of Geobacillus stearothermophilus 98
Extremophiles
10
321-326
2006
Geobacillus stearothermophilus (P85513), Geobacillus stearothermophilus, Geobacillus stearothermophilus 98 (P85513), Geobacillus stearothermophilus 98
Manually annotated by BRENDA team
Derekova, A.; Atanassova, M.; Christova, P.; Tchorbanov, B.; Shosheva, A.; Mandeva, R.; Rodrguez-Alonso, P.; Garabal, J.I.; Kambourova, M.
Physicochemical characteristics of a thermostable gellan lyase from Geobacillus stearothermophilus 98
Z. Naturforsch. C
65
231-238
2010
Geobacillus stearothermophilus (P85513), Geobacillus stearothermophilus 98 (P85513), Geobacillus stearothermophilus 98
Manually annotated by BRENDA team