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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-
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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
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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, 40°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
substrate polyG, pH 7.0, 50°C
24
substrate polyM, pH 7.0, 50°C
32
substrate alginate, pH 7.0, 50°C
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