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Information on EC 4.2.2.26 - oligo-alginate lyase
for references in articles please use BRENDA:EC4.2.2.26
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EC Tree 4 Lyases
4.2 Carbon-oxygen lyases
4.2.2 Acting on polysaccharides
4.2.2.26 oligo-alginate lyase
IUBMB Comments
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 β-elimination reaction, generating a new unsaturated non-reducing end after removal of the pre-existing one.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 4.2.2.26
- oligoalginate
- polysaccharide
-
biofuels
- degradation
- polyg
- seaweed
-
saccharification
-
exolytic
- lyases
- shewanella
-
metagenomics
- synthesis
Reaction Schemes
showCleavage 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
Synonyms
oalc6, oalc17, oals17, oligo-alginate lyase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Alg17C
AlyA3
Oal
oligoalginate lyase
Smlt2602
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REACTION
REACTION DIAGRAM
COMMENTARY
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
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alginate + H2O
?
Substrates: -
Products: enzyme degrades alginate more efficiently than polyM and polyG block into a monomeric sugar acid
Products: enzyme degrades alginate more efficiently than polyM and polyG block into a monomeric sugar acid
?
algino-oligosaccharide
unsaturated algino-monosaccharides
-
Substrates: -
Products: -
Products: -
?
algino-polysaccharide
unsaturated algino-monosaccharides
-
Substrates: -
Products: -
Products: -
?
hexa(beta-(1->4)-D-mannuronate)
monosaccharides + disaccharides + trisaccharides + tetrasaccharides + pentasaccharides
Substrates: -
Products: -
Products: -
?
penta(beta-(1->4)-D-mannuronate)
monosaccharides + disaccharides + trisaccharides + tetrasaccharides + pentasaccharides
Substrates: -
Products: -
Products: -
?
poly(alpha-(1->4)-L-guluronate)
disaccharides + trisaccharides + tetrasaccharides + pentasaccharides + hexasaccharides
poly(alpha-1,4-L-guluronate)
?
Cellulophaga sp. SY116
A0A345ANR9, A0A345ANS0
Substrates: -
Products: -
Products: -
?
poly(alpha-L-1,4-guluronate)
monosaccharides + disaccharides + trisaccharides
Vibrio sp. SY01
-
Substrates: less than 20% activity compared to poly(beta-(1->4)-D-mannuronate)
Products: -
Products: -
?
poly(beta-(1,4)-D-mannuronic acid/alpha-(1,4)-L-guluronic acid)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronic acid + 4-deoxy-beta-D-erythro-hex-4-enopyranuronic acid
poly(beta-(1->4)-D-mannuronate)
disaccharides + trisaccharides + tetrasaccharides + pentasaccharides + hexasaccharides
poly(beta-(1->4)-D-mannuronate)
monosaccharides + disaccharides + trisaccharides
Vibrio sp. SY01
-
Substrates: 100% activity
Products: -
Products: -
?
poly(beta-(1->4)guluronate) + H2O
?
Substrates: i.e. linear block polymer of alpha-L-guluronic acid
Products: -
Products: -
?
poly(beta-(1->4)mannuronate) + H2O
?
Substrates: i.e. linear block polymer of beta-D-mannuronic acid
Products: -
Products: -
?
poly(beta-1,4-D-mannuronate)
?
Cellulophaga sp. SY116
A0A345ANR9, A0A345ANS0
Substrates: -
Products: -
Products: -
?
poly-alpha-L-guluronate
?
A0A7L7K5T5
Substrates: lowest activity
Products: -
Products: -
?
sodium alginate
4-deoxy-L-erythro-4-hexenopyranouronate monomers
A0A7L7K5T5
Substrates: highest activity
Products: -
Products: -
?
sodium alginate
disaccharides + trisaccharides + tetrasaccharides + pentasaccharides + hexasaccharides
sodium alginate
monosaccharides + disaccharides + trisaccharides
Vibrio sp. SY01
-
Substrates: about 40% activity compared to poly(beta-(1->4)-D-mannuronate). The exo-type enzyme yields alginate monomers as the main product and recognizes alginate disaccharides as the minimal substrate
Products: -
Products: -
?
tetra(beta-(1->4)-D-mannuronate)
monosaccharides + disaccharides + trisaccharides + tetrasaccharides + pentasaccharides
tri(beta-(1->4)-D-mannuronate)
monosaccharides + disaccharides + trisaccharides + tetrasaccharides + pentasaccharides
Substrates: -
Products: -
Products: -
?
alginate
unsaturated algino-monosaccharides
Cellulophaga sp. SY116
A0A345ANR9, A0A345ANS0
Substrates: -
Products: -
Products: -
?
alginate
unsaturated algino-monosaccharides
Substrates: -
Products: alginate substrate is almost completely depolymerized into monosaccharides
Products: alginate substrate is almost completely depolymerized into monosaccharides
?
alginate
unsaturated algino-monosaccharides
Substrates: -
Products: enzyme completely degrades alginate into unsaturated uronate monomer
Products: enzyme completely degrades alginate into unsaturated uronate monomer
?
alginate
unsaturated algino-monosaccharides
Substrates: -
Products: -
Products: -
?
alginate
unsaturated algino-monosaccharides
Substrates: -
Products: -
Products: -
?
alginate
unsaturated algino-monosaccharides
Substrates: -
Products: enzyme completely degrades alginate into unsaturated uronate monomer
Products: enzyme completely degrades alginate into unsaturated uronate monomer
?
di(beta-(1->4)-D-mannuronate)
monosaccharides + disaccharides
Substrates: -
Products: -
Products: -
?
di(beta-(1->4)-D-mannuronate)
monosaccharides + disaccharides
Zobellia galactanivorans DsijT
Substrates: -
Products: -
Products: -
?
oligoalginate
unsaturated monosaccharides
Substrates: -
Products: -
Products: -
?
oligoalginate
unsaturated monosaccharides
Substrates: -
Products: -
Products: -
?
oligoalginate + H2O
4-deoxy-L-erythro-5-hexoseulose uronic acid
-
Substrates: -
Products: 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
Products: 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
?
oligoalginate + H2O
4-deoxy-L-erythro-5-hexoseulose uronic acid
Saccharophagus degradans 2-40 / ATCC 43961
-
Substrates: -
Products: 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
Products: 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
?
poly(alpha-(1->4)-L-guluronate)
disaccharides + trisaccharides + tetrasaccharides + pentasaccharides + hexasaccharides
Substrates: faint activity
Products: -
Products: -
?
poly(alpha-(1->4)-L-guluronate)
disaccharides + trisaccharides + tetrasaccharides + pentasaccharides + hexasaccharides
Zobellia galactanivorans DsijT
Substrates: faint activity
Products: -
Products: -
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronic acid
Substrates: -
Products: -
Products: -
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronic acid
Substrates: -
Products: -
Products: -
?
poly(beta-(1,4)-D-mannuronic acid/alpha-(1,4)-L-guluronic acid)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronic acid + 4-deoxy-beta-D-erythro-hex-4-enopyranuronic acid
Substrates: -
Products: -
Products: -
?
poly(beta-(1,4)-D-mannuronic acid/alpha-(1,4)-L-guluronic acid)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronic acid + 4-deoxy-beta-D-erythro-hex-4-enopyranuronic acid
Substrates: -
Products: -
Products: -
?
poly(beta-(1,4)glucuronate)
4-deoxy-alpha-L-threo-hex-4-enopyranuronic acid
Substrates: -
Products: -
Products: -
?
poly(beta-(1,4)glucuronate)
4-deoxy-alpha-L-threo-hex-4-enopyranuronic acid
Substrates: -
Products: -
Products: -
?
poly(beta-(1,4)guluronate)
4-deoxy-beta-D-erythro-hex-4-enopyranuronic acid
Substrates: -
Products: -
Products: -
?
poly(beta-(1,4)guluronate)
4-deoxy-beta-D-erythro-hex-4-enopyranuronic acid
Substrates: -
Products: -
Products: -
?
poly(beta-(1->4)-D-mannuronate)
disaccharides + trisaccharides + tetrasaccharides + pentasaccharides + hexasaccharides
Substrates: the enzyme AlyA3 is exolytic and highly specific for mannuronate stretches
Products: -
Products: -
?
poly(beta-(1->4)-D-mannuronate)
disaccharides + trisaccharides + tetrasaccharides + pentasaccharides + hexasaccharides
Zobellia galactanivorans DsijT
Substrates: the enzyme AlyA3 is exolytic and highly specific for mannuronate stretches
Products: -
Products: -
?
poly(beta-(1->4)-D-mannuronate)
unsaturated monosaccharides
Substrates: best substrate
Products: -
Products: -
?
poly(beta-(1->4)-D-mannuronate)
unsaturated monosaccharides
Substrates: best substrate
Products: -
Products: -
?
sodium alginate
disaccharides + trisaccharides + tetrasaccharides + pentasaccharides + hexasaccharides
Substrates: -
Products: -
Products: -
?
sodium alginate
disaccharides + trisaccharides + tetrasaccharides + pentasaccharides + hexasaccharides
Zobellia galactanivorans DsijT
Substrates: -
Products: -
Products: -
?
sodium alginate
unsaturated monosaccharides
Substrates: -
Products: -
Products: -
?
sodium alginate
unsaturated monosaccharides
Substrates: -
Products: -
Products: -
?
tetra(beta-(1->4)-D-mannuronate)
monosaccharides + disaccharides + trisaccharides + tetrasaccharides + pentasaccharides
Substrates: -
Products: -
Products: -
?
tetra(beta-(1->4)-D-mannuronate)
monosaccharides + disaccharides + trisaccharides + tetrasaccharides + pentasaccharides
Zobellia galactanivorans DsijT
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates: alginate, poly(beta-(1->4)-D-mannuronate), poly(alpha-(1->4)-L-guluronate)
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: starch, agarose and agar
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme possesses catalytic domains for both inherent endolytic and exolytic activities
Products: -
Products: -
-
additional information
?
-
Substrates: no substrates: starch, agarose and agar
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme possesses catalytic domains for both inherent endolytic and exolytic activities
Products: -
Products: -
-
additional information
?
-
A0A7L7K5T5
Substrates: the enzyme is exolytic and cleaves from the nonreducing end and shows no activity with heparin, chondroitin, and laminarin
Products: -
Products: -
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
oligoalginate + H2O
4-deoxy-L-erythro-5-hexoseulose uronic acid
-
Substrates: -
Products: 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
Products: 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
?
oligoalginate + H2O
4-deoxy-L-erythro-5-hexoseulose uronic acid
Saccharophagus degradans 2-40 / ATCC 43961
-
Substrates: -
Products: 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
Products: 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
LITERATURE
Ca2+
Mg2+
Mn2+
Na+
NaCl
additional information
the addition of calcium, lithium or magnesium does not affect the enzyme activity
NaCl
10 mM, 147% of initial activity, 300 mM, 276% of initial activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Mn2+
Cellulophaga sp. SY116
A0A345ANR9, A0A345ANS0
1 mM, 63% of initial activity; 1 mM, 63% of initial activity
NaCl
the enzyme loses 54% of its activity after the addition of 100 mM NaCl, and 2% of activity remain at 500 mM NaCl
Al3+
Cellulophaga sp. SY116
A0A345ANR9, A0A345ANS0
1 mM, 35% of initial activity; 1 mM, 62% of initial activity
Cu2+
Cellulophaga sp. SY116
A0A345ANR9, A0A345ANS0
1 mM, 40% of initial activity; 1 mM, 54% of initial activity
EDTA
Cellulophaga sp. SY116
A0A345ANR9, A0A345ANS0
1 mM, 22% of initial activity; 1 mM, 43% of initial activity
Fe3+
Cellulophaga sp. SY116
A0A345ANR9, A0A345ANS0
1 mM, 24% of initial activity; 1 mM, 36% of initial activity
Ni2+
Cellulophaga sp. SY116
A0A345ANR9, A0A345ANS0
1 mM, 57% of initial activity; 1 mM, 66% of initial activity
SDS
Cellulophaga sp. SY116
A0A345ANR9, A0A345ANS0
1 mM, 62% of initial activity; 1 mM, 68% of initial activity
Zn2+
Cellulophaga sp. SY116
A0A345ANR9, A0A345ANS0
1 mM, 48% of initial activity; 1 mM, 61% of initial activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.41
poly(beta-(1,4)-D-mannuronate)
wild-type, pH 8.0, 25°C
0.41
poly(beta-(1,4)-D-mannuronate)
mutant H208F, pH 8.0, 25°C
0.57
poly(beta-(1,4)-D-mannuronic acid/alpha-(1,4)-L-guluronic acid)
wild-type, pH 8.0, 25°C
-
0.98
poly(beta-(1,4)-D-mannuronic acid/alpha-(1,4)-L-guluronic acid)
mutant H208F, pH 8.0, 25°C
-
0.57
poly(beta-(1,4)glucuronate)
mutant H208F, pH 8.5, 25°C
-
1.4
poly(beta-(1,4)glucuronate)
wild-type, pH 8.5, 25°C
-
2.22
poly(beta-(1,4)guluronate)
mutant H208F, pH 8.0, 25°C
-
5.99
poly(beta-(1,4)guluronate)
wild-type, pH 8.0, 25°C
-
additional information
oligoalginate
-
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
21.3
poly(beta-(1,4)-D-mannuronate)
mutant H208F, pH 8.0, 25°C
62.2
poly(beta-(1,4)-D-mannuronate)
wild-type, pH 8.0, 25°C
2
poly(beta-(1,4)-D-mannuronic acid/alpha-(1,4)-L-guluronic acid)
mutant H208F, pH 8.0, 25°C
-
22.2
poly(beta-(1,4)-D-mannuronic acid/alpha-(1,4)-L-guluronic acid)
wild-type, pH 8.0, 25°C
-
0.4
poly(beta-(1,4)glucuronate)
wild-type, pH 8.5, 25°C
-
6.1
poly(beta-(1,4)glucuronate)
mutant H208F, pH 8.5, 25°C
-
1.4
poly(beta-(1,4)guluronate)
mutant H208F, pH 8.0, 25°C
-
34.6
poly(beta-(1,4)guluronate)
wild-type, pH 8.0, 25°C
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
51.5
poly(beta-(1,4)-D-mannuronate)
mutant H208F, pH 8.0, 25°C
151.8
poly(beta-(1,4)-D-mannuronate)
wild-type, pH 8.0, 25°C
2.1
poly(beta-(1,4)-D-mannuronic acid/alpha-(1,4)-L-guluronic acid)
mutant H208F, pH 8.0, 25°C
-
38.7
poly(beta-(1,4)-D-mannuronic acid/alpha-(1,4)-L-guluronic acid)
wild-type, pH 8.0, 25°C
-
0.3
poly(beta-(1,4)glucuronate)
wild-type, pH 8.5, 25°C
-
10.6
poly(beta-(1,4)glucuronate)
mutant H208F, pH 8.5, 25°C
-
0.7
poly(beta-(1,4)guluronate)
mutant H208F, pH 8.0, 25°C
-
additional information
alginate
Cellulophaga sp. SY116
A0A345ANR9
kcat/Km value 114.4 ml/mg/s, pH 7.0, 40°C
additional information
alginate
Cellulophaga sp. SY116
A0A345ANS0
kcat/Km value 114.4 ml/mg/s, pH 7.0, 40°C
additional information
alginate
Cellulophaga sp. SY116
A0A345ANR9
kcat/Km value 118.8 ml/mg/s, pH 7.0, 40°C
additional information
alginate
Cellulophaga sp. SY116
A0A345ANS0
kcat/Km value 118.8 ml/mg/s, pH 7.0, 40°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12.6
Cellulophaga sp. SY116
A0A345ANR9, A0A345ANS0
substrate poly(beta-1,4-D-mannuronate), pH 7.0, 40°C
76.8
Cellulophaga sp. SY116
A0A345ANR9, A0A345ANS0
substrate poly(alpha-1,4-L-guluronate), pH 7.0, 40°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
A0A7L7K5T5
the enzyme has a broad pH optimum in the region of pH 5.0 to 6.0. At acidic pH, there is a dramatic shift from no activity at pH 4.3 to almost maximal activity at pH 4.8
6.5 - 8
the buffer has a strong impact on enzymatic activity; it is highest with HEPES (pH 8.0 and 7.5) and with Tris-HCl at pH 7.0. Below pH 6.5, 20% of activity remains, and it is completely abolished at pH 9.0 and above
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
40
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 40
activity increases linearly with temperature between 10 and 40°C and decreases rapidly until being almost abolished at 50°C. The enzyme shows more than 70% activity between 25°C and 40°C
70 - 90
A0A7L7K5T5
the enzyme shows more than 80% activity from 70 to 90°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
Cellulophaga sp. SY116
A0A345ANR9, A0A345ANS0
enzyme degrades both alginate polymers and oligomers into monomers in an exolytic mode. Isoform OalC6 prefers alpha-L-guluronate blocks, while isoform OalC17 prefers poly beta-D-mannuronate blocks. The combination of OalC6 and OalC17 shows synergistic degradation ability toward both alginate polymers and oligomers
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). EALGL_STRMK
Stenotrophomonas maltophilia (strain K279a)
742
0
82406
Swiss-Prot
-
EALGL_SACD2
Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024)
736
0
81582
Swiss-Prot
Secretory Pathway (Reliability: 1)
A9CEJ9_AGRFC
Agrobacterium fabrum (strain C58 / ATCC 33970)
776
0
87871
TrEMBL
-
G0LCA3_ZOBGA
Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)
751
0
85054
TrEMBL
other Location (Reliability: 1)
G1EH67_9SPHN
731
0
79953
TrEMBL
Secretory Pathway (Reliability: 5)
T1RPY0_STEMA
742
0
82081
TrEMBL
other Location (Reliability: 4)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
?
Cellulophaga sp. SY116
A0A345ANR9, A0A345ANS0
x * 85900, calculated from sequence, x * 85000, SDS-PAGE
?
Cellulophaga sp. SY116
A0A345ANR9, A0A345ANS0
x * 85700, calculated from sequence, x * 85000, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
sequence contains a putative signal peptide of 44 amino acid residues
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild type and mutant enzyme Y274A in complex with oligo-mannuronate, hanging drop vapor diffusion method
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R236A
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
E644A
the exolytic activity of the mutant decreases to 77.6% compared to the wild type enzyme
H208F
in addition to cleaving alginate-based substrates, mutant displays significant exolytic glucuronan activity
R241A
the exolytic activity of the mutant decreases to 43.1% compared to the wild type enzyme
R241A/E644A
the exolytic activity of the mutant decreases to 61.5% compared to the wild type enzyme
R418A
the mutant loses almost all alginate degradation activity compared to the wild type enzyme
Y238F
the exolytic activity of the mutant decreases to 8.1% compared to the wild type enzyme
Y455F
significantly diminished yet measurable activity toward alginate and M and G blocks
H208F
-
in addition to cleaving alginate-based substrates, mutant displays significant exolytic glucuronan activity
-
Y455F
-
significantly diminished yet measurable activity toward alginate and M and G blocks
-
E644A
-
the exolytic activity of the mutant decreases to 77.6% compared to the wild type enzyme
-
R241A
-
the exolytic activity of the mutant decreases to 43.1% compared to the wild type enzyme
-
R241A/E644A
-
the exolytic activity of the mutant decreases to 61.5% compared to the wild type enzyme
-
R418A
-
the mutant loses almost all alginate degradation activity compared to the wild type enzyme
-
Y238F
-
the exolytic activity of the mutant decreases to 8.1% compared to the wild type enzyme
-
Y251A
A0A7L7K5T5
inactive with poly-alpha-L-guluronate and strongly reduced activity with poly-beta-D-mannuronate and alginate, compared to the wild type enzyme
R231A
Vibrio sp. SY01
-
compared to the wild type, the mutation causes a significant reduction in substrate affinity for poly(beta-(1->4)-D-mannuronate) blocks. However, the mutation does not induce a drastic change in affinity for poly(alpha-L-1,4-guluronate) blocks
R231F
Vibrio sp. SY01
-
compared to the wild type, the mutation causes a significant reduction in substrate affinity for poly(beta-(1->4)-D-mannuronate) blocks. However, the mutation does not induce a drastic change in affinity for poly(alpha-L-1,4-guluronate) blocks
R231H
Vibrio sp. SY01
-
compared to the wild type, the mutation causes a significant reduction in substrate affinity for poly(beta-(1->4)-D-mannuronate) blocks. However, the mutation does not induce a drastic change in affinity for poly(alpha-L-1,4-guluronate) blocks
R231K
Vibrio sp. SY01
-
compared to the wild type, the mutation causes a significant reduction in substrate affinity for poly(beta-(1->4)-D-mannuronate) blocks. However, the mutation does not induce a drastic change in affinity for poly(alpha-L-1,4-guluronate) blocks
R231S
Vibrio sp. SY01
-
compared to the wild type, the mutation causes a significant reduction in substrate affinity for poly(beta-(1->4)-D-mannuronate) blocks. However, the mutation does not induce a drastic change in affinity for poly(alpha-L-1,4-guluronate) blocks
H200A
the mutation strongly impairs the enzyme activity to 13.9% of wild type
Y274A
the mutation virtually abolishes the enzyme activity to 0.2% of wild type
Y466A
the mutation virtually abolishes the enzyme activity to 0.4% of wild type
H200A
Zobellia galactanivorans DsijT
-
the mutation strongly impairs the enzyme activity to 13.9% of wild type
-
Y274A
Zobellia galactanivorans DsijT
-
the mutation virtually abolishes the enzyme activity to 0.2% of wild type
-
Y466A
Zobellia galactanivorans DsijT
-
the mutation virtually abolishes the enzyme activity to 0.4% of wild type
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.4 - 8
Vibrio sp. SY01
-
the enzyme retains over 70% of its initial activity after incubation for 12 h at pH 3.4-8.0
6 - 8
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
40 - 60
Vibrio sp. SY01
-
74.5, 61.2, and 47.6% of the enzymatic activity remain after incubation for 1 h at 40, 50, and 60°C, respectively
60 - 65
A0A7L7K5T5
the enzyme is stable for 24 h at 60°C, while its activity declines during preincubation at 65°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Superdex 200 gel filtration
Ni-Sepharose column chromatography, and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
synthesis
saccharification of alginate into alginate monosaccharides. Unsaturated monosaccharides up to 3.3 mg/ml are successfully prepared from 1% (w/v) alginate by using the recombinant oligoalginate lyase of Sphingomonas sp. MJ-3
degradation
Cellulophaga sp. SY116
A0A345ANR9, A0A345ANS0
combining exotype alginate lyases OalC6 and OalC17 and the endotype alginate lyase AlySY08 enables the production of alginate monomers due to synergistic processes
degradation
enzymatical saccharification of acid pretreated and untreated brown macroalgae, first at pH 7.5, 25°C for 12 h with a blend of recombinant alginate and oligoalginate lyases, then at pH 5.2 using a commercial cellulase cocktail. The use of recombinant alginate lyases and oligoalginate lyases in combination with cellulases increases the release of glucose from untreated seaweed. For saccharification of pretreated algae, only cellulases are needed to achieve high glucose yields
degradation
-
enzymatical saccharification of acid pretreated and untreated brown macroalgae, first at pH 7.5, 25°C for 12 h with a blend of recombinant alginate and oligoalginate lyases, then at pH 5.2 using a commercial cellulase cocktail. The use of recombinant alginate lyases and oligoalginate lyases in combination with cellulases increases the release of glucose from untreated seaweed. For saccharification of pretreated algae, only cellulases are needed to achieve high glucose yields
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hashimoto, W.; Miyake, O.; Momma, K.; Kawai, S.; Murata, K.
Molecular identification of oligoalginate lyase of Sphingomonas sp. strain A1 as one of the enzymes required for complete depolymerization of alginate
J. Bacteriol.
182
4572-4577
2000
Sphingomonas sp.
brenda
Suzuki, H.; Suzuki, K.; Inoue, A.; Ojima, T.
A novel oligoalginate lyase from abalone, Haliotis discus hannai, that releases disaccharide from alginate polymer in an exolytic manner
Carbohydr. Res.
341
1809-1819
2006
Haliotis discus hannai
brenda
Kim, H.T.; Chung, J.H.; Wang, D.; Lee, J.; Woo, H.C.; Choi, I.G.; Kim, K.H.
Depolymerization of alginate into a monomeric sugar acid using Alg17C, an exo-oligoalginate lyase cloned from Saccharophagus degradans 2-40
Appl. Microbiol. Biotechnol.
93
2233-2239
2012
Saccharophagus degradans, Saccharophagus degradans 2-40 / ATCC 43961
brenda
Wang,L.; Li, S.; Yu, W.; Gong, Q.
Cloning, overexpression and characterization of a new oligoalginate lyase from a marine bacterium, Shewanella sp.
Biotechnol. Lett.
37
665-671
2015
Shewanella sp. (A0A088CA41)
brenda
Ryu, M.; Lee, E.
Saccharification of alginate by using exolytic oligoalginate lyase from marine bacterium Sphingomonas sp. MJ-3
J. Ind. Eng. Chem.
17
853-858
2011
Sphingomonas sp. (G1EH67)
-
brenda
Shin, J.W.; Lee, O.K.; Park, H.H.; Kim, H.S.; Lee, E.Y.
Molecular characterization of a novel oligoalginate lyase consisting of AlgL- and heparinase II/III-like domains from Stenotrophomonas maltophilia KJ-2 and its application to alginate saccharification
Korean J. Chem. Engin.
32
917-924
2015
Stenotrophomonas maltophilia (T1RPY0), Stenotrophomonas maltophilia KJ-2 (T1RPY0)
-
brenda
Kim, H.S.; Chu, Y.J.; Park, C.-H.; Lee, E.Y.; Kim, H.S.
Site-directed mutagenesis-based functional analysis and characterization of endolytic lyase activity of N- and C-terminal domains of a novel oligoalginate lyase from Sphingomonas sp. MJ-3 possessing exolytic lyase activity in the intact enzyme
Mar. Biotechnol.
17
782-792
2015
Sphingomonas sp. (G1EH67)
brenda
Ravanal, M.; Sharma, S.; Gimpel, J.; Reveco-Urzua, F.; Overland, M.; Horn, S.; Lienqueo, M.
The role of alginate lyases in the enzymatic saccharification of brown macroalgae, Macrocystis pyrifera and Saccharina latissima
Algal Res.
26
287-293
2017
Agrobacterium fabrum (A9CEJ9), Agrobacterium fabrum ATCC 33970 (A9CEJ9)
-
brenda
MacDonald, L.C.; Weiler, E.B.; Berger, B.W.
Engineering broad-spectrum digestion of polyuronides from an exolytic polysaccharide lyase
Biotechnol. Biofuels
9
43
2016
Stenotrophomonas maltophilia (B2FSW8), Stenotrophomonas maltophilia K279a (B2FSW8)
brenda
Li, S.; Wang, L.; Chen, X.; Zhao, W.; Sun, M.; Han, Y.
Cloning, expression, and biochemical characterization of two new oligoalginate lyases with synergistic degradation capability
Mar. Biotechnol.
20
75-86
2018
Cellulophaga sp. SY116 (A0A345ANR9), Cellulophaga sp. SY116 (A0A345ANS0)
brenda
Arntzen, M.O.; Pedersen, B.; Klau, L.J.; Stokke, R.; Oftebro, M.; Antonsen, S.G.; Fredriksen, L.; Sletta, H.; Aarstad, O.A.; Aachmann, F.L.; Horn, S.J.; Eijsink, V.G.H.
Alginate degradation insights obtained through characterization of a thermophilic exolytic alginate lyase
Appl. Environ. Microbiol.
87
e02399-20
2021
uncultured bacterium (A0A7L7K5T5)
brenda
Chu, Y.; Kim, H.; Kim, M.; Lee, E.; Kim, H.
Functional characterization of a novel oligoalginate lyase of Stenotrophomonas maltophilia KJ-2 using site-specific mutation reveals bifunctional mode of action, possessing both endolytic and exolytic degradation activity toward alginate in seaweed biomas
Front. Mar. Sci.
7
420
2020
Stenotrophomonas maltophilia (T1RPY0), Stenotrophomonas maltophilia KJ-2 (T1RPY0)
-
brenda
Li, S.; Wang, L.; Jung, S.; Lee, B.S.; He, N.; Lee, M.S.
Biochemical characterization of a new oligoalginate lyase and its biotechnological application in Laminaria japonica degradation
Front. Microbiol.
11
316
2020
Vibrio sp. SY01
brenda
Jouanneau, D.; Klau, L.J.; Larocque, R.; Jaffrennou, A.; Duval, G.; Le Duff, N.; Roret, T.; Jeudy, A.; Aachmann, F.L.; Czjzek, M.; Thomas, F.
Structure-function analysis of a new PL17 oligoalginate lyase from the marine bacterium Zobellia galactanivorans DsijT
Glycobiology
31
1364-1377
2021
Zobellia galactanivorans (G0LCA3), Zobellia galactanivorans DsijT (G0LCA3)
brenda
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