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EC Tree
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.
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,
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alginate lyase VI
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mannuronate alginate lyase
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poly(1,4-beta-D-mannuronide) lyase
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poly(beta-D-1,4-mannuronide) lyase
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Poly(beta-D-mannuronate) lyase
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Poly(mana) alginate lyase
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poly(mana)alginate lyase
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additional information
the enzyme belongs to the polysaccharide-lyase-family 14, PL-14
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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.
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alginate
unsaturated algino-oligosaccharides
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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)
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)
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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)
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additional information
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additional information
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substrate is sodium alginate originating from Macrocystis pyrifera, preparation of poly(M)-rich, poly(G)-rich, and random substrates thereof
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additional information
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substrate is sodium alginate originating from Macrocystis pyrifera, preparation of poly(M)-rich, poly(G)-rich, and random substrates thereof
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Bacterial Infections
Genetically engineered alginate lyase-PEG conjugates exhibit enhanced catalytic function and reduced immunoreactivity.
Bacterial Infections
Hyaluronan-cholesterol nanohydrogels: Characterisation and effectiveness in carrying alginate lyase.
Communicable Diseases
Preparation and properties of alginate lyase modified with poly(ethylene glycol).
Cystic Fibrosis
Alginate lyase and ciprofloxacin co-immobilization on biopolymeric microspheres for cystic fibrosis treatment.
Cystic Fibrosis
Alginate lyase enhances antibiotic killing of mucoid Pseudomonas aeruginosa in biofilms.
Cystic Fibrosis
Alginate lyase immobilized chitosan nanoparticles of ciprofloxacin for the improved antimicrobial activity against the biofilm associated mucoid P. aeruginosa infection in cystic fibrosis.
Cystic Fibrosis
Cellulophaga algicola alginate lyase inhibits biofilm formation of a clinical Pseudomonas aeruginosa strain MCC 2081.
Cystic Fibrosis
Genetically engineered alginate lyase-PEG conjugates exhibit enhanced catalytic function and reduced immunoreactivity.
Cystic Fibrosis
Impact of alginate-producing Pseudomonas aeruginosa on alveolar macrophage apoptotic cell clearance.
Cystic Fibrosis
Modeling and Re-Engineering of Azotobacter vinelandii Alginate Lyase to Enhance Its Catalytic Efficiency for Accelerating Biofilm Degradation.
Cystic Fibrosis
Molecular modeling and redesign of alginate lyase from Pseudomonas aeruginosa for accelerating CRPA biofilm degradation.
Cystic Fibrosis
Sequence of a gene encoding a (poly ManA) alginate lyase active on Pseudomonas aeruginosa alginate.
Cystic Fibrosis
The effect of alginate lyase on the gentamicin resistance of Pseudomonas aeruginosa in mucoid biofilms.
Cysts
Characterization of three new Azotobacter vinelandii alginate lyases, one of which is involved in cyst germination.
Infections
Alginate lyase immobilized chitosan nanoparticles of ciprofloxacin for the improved antimicrobial activity against the biofilm associated mucoid P. aeruginosa infection in cystic fibrosis.
Infections
Disruption of the extracellular polymeric network of Pseudomonas aeruginosa biofilms by alginate lyase enhances pathogen eradication by antibiotics.
Infections
Molecular modeling and redesign of alginate lyase from Pseudomonas aeruginosa for accelerating CRPA biofilm degradation.
Infections
Proteomic and Transcriptomic Analysis of Microviridae ?X174 Infection Reveals Broad Upregulation of Host Escherichia coli Membrane Damage and Heat Shock Responses.
Infections
Structural Dynamics and Topology of the Inactive Form of S21 Holin in a Lipid Bilayer Using Continuous-Wave Electron Paramagnetic Resonance Spectroscopy.
Pseudomonas Infections
Molecular modeling and redesign of alginate lyase from Pseudomonas aeruginosa for accelerating CRPA biofilm degradation.
Pulmonary Disease, Chronic Obstructive
Impact of alginate-producing Pseudomonas aeruginosa on alveolar macrophage apoptotic cell clearance.
Tuberculosis
High precision multi-genome scale reannotation of enzyme function by EFICAz.
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additional information
alginate
additional information
alginate
Km value 0.95 mg/ml, wild-type, pH 7.0, 30°C
additional information
poly(beta-(1,4)-D-mannuronate)
Km value 0.79 mg/ml, wild-type, pH 7.0, 30°C
additional information
poly(beta-(1,4)-D-mannuronate/alpha-(1,4)-L-guluronate)
Km value 68.8 mg/ml, wild-type, pH 7.0, 30°C
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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
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substrate poly(beta-(1,4)-D-mannuronate), wild-type, pH 7.0, 30°C
5796
purified native AkAly30, pH 8.0, 30°C
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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
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additional information
residue N120 is not directly related to the pH-dependence of AkAly30, overview
additional information
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residue N120 is not directly related to the pH-dependence of AkAly30, overview
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UniProt
brenda
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brenda
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brenda
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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
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E7FLQ2_APLKU
295
0
33035
TrEMBL
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29722
x * 29722, sequence calculation, x * 30000, SDS-PAGE
30000
x * 29722, sequence calculation, x * 30000, SDS-PAGE
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x * 29722, sequence calculation, x * 30000, SDS-PAGE
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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
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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
site-directed mutagenesis, the mutation highly reduces the enzyme activity compared to the wild-type enzyme
Y140F
mutation in active site residue, 1.3% of wild-type activity
Y142F
site-directed mutagenesis, the mutation highly reduces the enzyme activity compared to the wild-type enzyme
Y142F
mutation in active site residue, 0.6% of wild-type activity
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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
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AkAly30 DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic analysis, expression in Escherichia coli strain BL21(DE3)
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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
brenda
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)
brenda