Information on EC 4.2.2.26 - oligo-alginate lyase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
4.2.2.26
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RECOMMENDED NAME
GeneOntology No.
oligo-alginate lyase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleavage of poly(4-deoxy-alpha-L-erythro-hexopyranuronoside) oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends into 4-deoxy-alpha-L-erythro-hex-4-enopyranuronate monosaccharides
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
alginate degradation
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SYSTEMATIC NAME
IUBMB Comments
alginate oligosaccharide 4-deoxy-alpha-L-erythro-hex-4-enopyranuronate-(1?4)-hexananopyranuronate lyase
The enzyme degrades unsaturated oligosaccharides produced by the action of alginate lyases (EC 4.2.2.3 and EC 4.2.2.11) on alginate, by repeatedly removing the unsaturated residue from the non-reducing end until only unsaturated monosaccharides are left. The enzyme catalyses a beta-elimination reaction, generating a new unsaturated non-reducing end after removal of the pre-existing one.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
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
alginate
unsaturated algino-monosaccharides
show the reaction diagram
alginate + H2O
?
show the reaction diagram
algino-oligosaccharide
unsaturated algino-monosaccharides
show the reaction diagram
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-
-
-
?
algino-polysaccharide
unsaturated algino-monosaccharides
show the reaction diagram
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-
-
-
?
oligoalginate
unsaturated monosaccharides
show the reaction diagram
oligoalginate + H2O
4-deoxy-L-erythro-5-hexoseulose uronic acid
show the reaction diagram
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enzyme preferentially acts on oligoalginates with degrees of polymerization higher than 2 to produce the alginate monomer, 4-deoxy-L-erythro-5-hexoseulose uronic acid
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?
poly(beta-(1->4)-D-mannuronate)
unsaturated monosaccharides
show the reaction diagram
poly(beta-(1->4)guluronate) + H2O
?
show the reaction diagram
poly(beta-(1->4)mannuronate) + H2O
?
show the reaction diagram
additional information
?
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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
oligoalginate + H2O
4-deoxy-L-erythro-5-hexoseulose uronic acid
show the reaction diagram
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enzyme preferentially acts on oligoalginates with degrees of polymerization higher than 2 to produce the alginate monomer, 4-deoxy-L-erythro-5-hexoseulose uronic acid
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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1.4- to 2fold stimulation
Fe2+
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1.4- to 2fold stimulation
KCl
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1 mM, 120% of initial activity
Mg2+
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1.4- to 2fold stimulation
Mn2+
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1.4- to 2fold stimulation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Al3+
1 mM, 56% residual activity
Ca2+
1 mM, 80% residual activity
Cu2+
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1 mM, 5% residual activity
EDTA
1 mM, 49% residual activity
Fe3+
1 mM, 44% residual activity
Hg2+
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1 mM, no residual activity
Ni2+
1 mM, 40% residual activity
SDS
1 mM, 34% residual activity
Zn2+
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1 mM, 30% residual activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
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1 mM, 7fold stimulation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
oligoalginate
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the KM and Vmax of Alg17C are 35.2 mg/ml and 41.7 U/mg, respectively, pH 6.0, 40C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
substrate polyG, pH 7.0, 50C
24
substrate polyM, pH 7.0, 50C
32
substrate alginate, pH 7.0, 50C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
79000
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x * 81600, calculated, x * 79000, SDS-PAGE
79900
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x * 79900, calculated
81600
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x * 81600, calculated, x * 79000, SDS-PAGE
82000
x * 82000, SDS-PAGE
85000
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x * 86543, calculated, x * 85000, SDS-PAGE
86543
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x * 86543, calculated, x * 85000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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733560
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H178A
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mutant shows reduced oligoalginate lyase activity
H389A
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mutant shows reduced oligoalginate lyase activity
N177A
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mutant shows reduced oligoalginate lyase activity
R236A
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mutant exhibits endolytic activity. The overexpressed mutant protein (79.6 kDa) is proteolytically cleaved into the N-terminal 32.0-kDa and the C-terminal 47.6-kDa fragments. Both fragments show endolytic lyase activity
Y234F
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mutant shows reduced oligoalginate lyase activity
Y426F
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mutant shows reduced oligoalginate lyase activity
H178A
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mutant shows reduced oligoalginate lyase activity
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N177A
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mutant shows reduced oligoalginate lyase activity
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R236A
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mutant exhibits endolytic activity. The overexpressed mutant protein (79.6 kDa) is proteolytically cleaved into the N-terminal 32.0-kDa and the C-terminal 47.6-kDa fragments. Both fragments show endolytic lyase activity
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Y234F
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mutant shows reduced oligoalginate lyase activity
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Y426F
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mutant shows reduced oligoalginate lyase activity
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis