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Information on EC 4.2.2.3 - mannuronate-specific alginate lyase

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.2 Acting on polysaccharides
                4.2.2.3 mannuronate-specific alginate lyase
IUBMB Comments
The enzyme catalyses the degradation of alginate by a beta-elimination reaction. It cleaves the (1->4) bond between beta-D-mannuronate and either alpha-L-guluronate or beta-D-mannuronate, generating oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at the reducing end. Depending on the composition of the substrate, the enzyme produces oligosaccharides ranging from two to four residues, with preference for shorter products. cf. EC 4.2.2.11, guluronate-specific alginate lyase.
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UNIPROT: E7FLQ2
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
alginate lyase, lysis protein, oligoalginate lyase, alg17c, a1-ii, aly-sj02, alg-5, a1-iii, hdaly, alypm, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alginate lyase
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alginate lyase I
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alginate lyase VI
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AlgL
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lyase, alginate
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mannuronate alginate lyase
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-
-
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poly(1,4-beta-D-mannuronide) lyase
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-
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poly(beta-D-1,4-mannuronide) lyase
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-
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Poly(beta-D-mannuronate) lyase
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-
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Poly(mana) alginate lyase
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-
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poly(mana)alginate lyase
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-
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SP2
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additional information
the enzyme belongs to the polysaccharide-lyase-family 14, PL-14
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
alginate beta-D-mannuronate-uronate lyase
The enzyme catalyses the degradation of alginate by a beta-elimination reaction. It cleaves the (1->4) bond between beta-D-mannuronate and either alpha-L-guluronate or beta-D-mannuronate, generating oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at the reducing end. Depending on the composition of the substrate, the enzyme produces oligosaccharides ranging from two to four residues, with preference for shorter products. cf. EC 4.2.2.11, guluronate-specific alginate lyase.
CAS REGISTRY NUMBER
COMMENTARY hide
86922-62-5
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9024-15-1
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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-oligosaccharides
show the reaction diagram
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-
-
?
poly(alpha-(1,4)-L-guluronate)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
show the reaction diagram
reaction of EC 4.2.2.11
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-
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
show the reaction diagram
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-
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?
poly(beta-(1,4)-D-mannuronate/alpha-(1,4)-L-guluronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate) + 4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
show the reaction diagram
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?
additional information
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
alginate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.01
substrate poly(alpha-(1,4)-L-guluronate), mutant G118N, pH 7.0, 30°C
0.03
substrate poly(alpha-(1,4)-L-guluronate), mutant C115A/C124G, pH 7.0, 30°C
0.08
substrate poly(beta-(1,4)-D-mannuronate/alpha-(1,4)-L-guluronate), mutant G118N, pH 7.0, 30°C
0.11
substrate alginate, mutant Y142F, pH 7.0, 30°C
0.16
substrate poly(alpha-(1,4)-L-guluronate), wild-type, pH 7.0, 30°C
0.18
substrate poly(beta-(1,4)-D-mannuronate), mutant G118N, pH 7.0, 30°C
0.22
substrate alginate, mutant Y140F, pH 7.0, 30°C
0.31
substrate alginate, mutant G118N, pH 7.0, 30°C
0.83
substrate poly(beta-(1,4)-D-mannuronate/alpha-(1,4)-L-guluronate), mutant C115A/C124G, pH 7.0, 30°C
17.4
substrate alginate, wild-type, pH 7.0, 30°C
2.2
substrate poly(beta-(1,4)-D-mannuronate/alpha-(1,4)-L-guluronate), wild-type, pH 7.0, 30°C
2100
purified recombinant His-tagged AkAly30, pH 8.0, 30°C
33
substrate poly(beta-(1,4)-D-mannuronate), wild-type, pH 7.0, 30°C
5796
purified native AkAly30, pH 8.0, 30°C
6
substrate alginate, mutant C115A/C124G, pH 7.0, 30°C
6.8
substrate poly(beta-(1,4)-D-mannuronate), mutant C115A/C124G, pH 7.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the polysaccharide-lyase-family 14, PL-14, primary structure analysis
physiological function
herbivorous marine gastropods such as abalone and sea hare ingest brown algae as a major diet and degrade the dietary alginate with alginate lyase in their digestive fluid
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
E7FLQ2_APLKU
295
0
33035
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29722
x * 29722, sequence calculation, x * 30000, SDS-PAGE
30000
x * 29722, sequence calculation, x * 30000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 29722, sequence calculation, x * 30000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure at 1.77 A resolution and putative substrate-binding model. The enzyme adopts a beta-jelly roll fold at the core of the structure and residues Lys99, Tyr140, and Tyr142 form catalytic residues in the active site
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C115A/C124G
strong loss of activity
G118N
almost complete loss of activity
K99A
site-directed mutagenesis, the mutation highly reduces the enzyme activity compared to the wild-type enzyme
N120H
site-directed mutagenesis, reverse replacement of N120 by His in recAkAly30 increases the activity at pH 10.0 from 8 U/mg to 93 U/mg. However, the activity level at pH 7.0, i.e., 774.8 U/mg, is still much higher than that at pH 10.0
R128A
site-directed mutagenesis, the mutation highly reduces the enzyme activity compared to the wild-type enzyme
S126A
site-directed mutagenesis, the mutation highly reduces the enzyme activity compared to the wild-type enzyme
Y140F
Y142F
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged AkAly30 33fold from Escherihcia coli strain BL21(DE3) by nickel affinity chromatography, native AkAly30 97.58fold by ammonium sulfate fractionation and cation exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
AkAly30 DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic analysis, expression in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rahman, M.M.; Inoue, A.; Tanaka, H.; Ojima, T.
cDNA cloning of an alginate lyase from a marine gastropod Aplysia kurodai and assessment of catalytically important residues of this enzyme
Biochimie
93
1720-1730
2011
Aplysia kurodai (E7FLQ2), Aplysia kurodai
Manually annotated by BRENDA team
Qin, H.M.; Miyakawa, T.; Inoue, A.; Nishiyama, R.; Nakamura, A.; Asano, A.; Sawano, Y.; Ojima, T.; Tanokura, M.
Structure and polymannuronate specificity of a eukaryotic member of polysaccharide lyase family 14
J. Biol. Chem.
292
2182-2190
2017
Aplysia kurodai (E7FLQ2)
Manually annotated by BRENDA team