Any feedback?
Information on EC 4.2.2.11 - guluronate-specific alginate lyase and Organism(s) Saccharophagus degradans and UniProt Accession Q21FJ0
for references in articles please use BRENDA:EC4.2.2.11Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
4.2.2.11 guluronate-specific alginate lyaseIUBMB Comments
The enzyme catalyses the degradation of alginate by a beta-elimination reaction. It cleaves the (1->4) bond between alpha-L-guluronate 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 alpha-L-guluronate at the reducing end. Depending on the composition of the substrate, the enzyme produces oligosaccharides ranging from two to six residues, with preference for shorter products. cf. EC 4.2.2.3, mannuronate-specific alginate lyase.
Specify your search results
Word Map
- 4.2.2.11
- lyases
- degradation
-
klebsiella
- unsaturated
- polysaccharide
-
endolytic
- pneumoniae
-
depolymerization
- synthesis
- aerogenes
- flavobacterium
-
4.2.2.3
- tetrasaccharide
- algae
-
terrestrial
-
mannuronate
- sphingomonas
- biomass
- biofuel production
- agriculture
- industry
- food industry
The taxonomic range for the selected organisms is: Saccharophagus degradans
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
algmytc, guluronate-specific alginate lyase, guluronate lyase, alya1pl7, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alginase II
-
-
-
-
guluronate lyase
-
-
-
-
L-guluronan lyase
-
-
-
-
L-guluronate lyase
-
-
-
-
lyase, polyguluronate
-
-
-
-
poly(1,4-alpha-L-guluronide)lyase
-
-
-
-
poly(alpha-L-guluronate) lyase
-
-
-
-
poly-alpha-L-guluronate lyase
-
-
-
-
polyguluronate-specific alginate lyase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and alpha-L-guluronate at their reducing end
substrate binding, structural change and exolytic mechanism of alginate depolymerization by Alg17c, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination of an alcohol from a polysaccharide
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
alginate alpha-L-guluronate-uronate lyase
The enzyme catalyses the degradation of alginate by a beta-elimination reaction. It cleaves the (1->4) bond between alpha-L-guluronate 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 alpha-L-guluronate at the reducing end. Depending on the composition of the substrate, the enzyme produces oligosaccharides ranging from two to six residues, with preference for shorter products. cf. EC 4.2.2.3, mannuronate-specific alginate lyase.
CAS REGISTRY NUMBER
COMMENTARY
64177-88-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alginate
?
-
the enzyme endolytically depolymerizes alginate by beta-elimination into oligo-alginates with degrees of polymerization of 2-5
-
-
?
additional information
?
-
the enzyme Alg17c is an exolytic alginate lyase, structure-function characterization of active site residues that are suggested to be involved in the exolytic mechanism of alginate depolymerization, overview
-
-
?
additional information
?
-
recombinant Alg17C preferentially acts on oligoalginates with degrees of polymerization higher than 2 to produce the alginate monomer, 4-deoxy-L-erythro-5-hexoseulose uronic acid. The enzyme can produce a monomeric sugar acid from alginate by the concerted action of an endo-type alginate lyase and exo-type alginate lyase Alg17C, substrate specificity of Alg17C, overview
-
-
?
additional information
?
-
the enzyme is active on poly-MM, poly-GG, and poly-MG substrates. Exolytic depolymerization of these polysaccharides by alginate lyase yields a monosaccharide and a product containing a DELTA-(4,5)-unsaturated uronic acid moiety. A mixture of alginate di-, tri-, and tetrasaccharides are processed into mono- and disaccharides in the presence of Alg17c. An alginate trisaccharide represents the minimal length substrate for Alg17c, complete processing only of the tri- and tetrasaccharide substrates, substrate specificity and binding structure, Fourier electron density map, overview
-
-
?
additional information
?
-
-
the enzyme is active on poly(alpha-L-guluronate) and poly(beta-D-mannuronate), cf. EC 4.2.2.3
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
the enzyme Alg17c is an exolytic alginate lyase, structure-function characterization of active site residues that are suggested to be involved in the exolytic mechanism of alginate depolymerization, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
relevance of this zinc ion in catalytic activity, metal-binding protein ligands are His533, Gln551, and Lys573. The metal ion establishes the orientation of His415 and Arg438, which would otherwise be mobile, to set these residues for interactions with substrate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
41.4
-
purified recombinant His-tagged enzyme, pH 7.0, 50°C, substrate alginate
46
-
purified recombinant His-tagged enzyme, substrate poly(alpha-L-guluronate), pH 7.0, 50°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
highest activity at pH 6.0, which sharply decreases when the pH is higher or lower than pH 6.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
evolution
-
the enzyme belongs to the to the polysaccharide lyase-7 family
evolution
the enzyme belongs to the polysaccharide lyase PL7 family. Structure and beta-elimination mechanism for glycolytic bond cleavage by Alg17c are similar to those observed for family 15 polysaccharide lyases and other lyases, evolutionary relationships and structure-based hierarchy in the classification, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
79100
x * 81600, about, sequence calculation, x * 79100, recombinant enzyme, SDS-PAGE
81600
x * 81600, about, sequence calculation, x * 79100, recombinant enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 81600, about, sequence calculation, x * 79100, recombinant enzyme, SDS-PAGE
homodimer
structure analysis, SDS-PAGE and analytical gel filtration, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant soluble His-tagged wild-type and selenomethionine-labeled enzyme, and two mutant enzymes H202L and Y258A, and Y258A DELTAMMG variant, free or in complex with an alginate trisaccharide, hanging drop vapour diffusion method, mixing of 15 mg/ml protein in in 20 mM HEPES, pH 7.5, 100 mM KCl, with 0.1 M Tris, pH 8.0, 5% 2-methyl-2,4-pentanediol, 10% PEG 6000, 3 days, 16°C, X-ray diffraction structure determination and analysis at 1.85 A, 1.7 A, 2.45 A, and 1.9 A resolution, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H202L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H415A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Q149A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R260A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R438A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant soluble His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) Rosetta culture supernatant by nickel affinity chromatography and gel filtration
recombinant His-tagged enzyme lacking the signal peptide from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
subcloning of His-tagged wild-type and mutant enzymes in Escherichia coli strain DH5-alpha, expression in Escherichia coli strain BL21(DE3) Rosetta, the enzymes are secreted from periplasmic space
gene alg7D, overexpression of soluble His-tagged enzyme lacking the signal peptide in Escherichia coli strain BL21(DE3)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
Alg17C can be used as the key enzyme to produce alginate monomers in the process of utilizing alginate for biofuels and chemicals production
synthesis
Alg17C can be used as the key enzyme to produce alginate monomers in the process of utilizing alginate for biofuels and chemicals production
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q21FJ0), Saccharophagus degradans 2-40 / ATCC 43961 (Q21FJ0)
Kim, H.T.; Ko, H.J.; Kim, N.; Kim, D.; Lee, D.; Choi, I.G.; Woo, H.C.; Kim, M.D.; Kim, K.H.
Characterization of a recombinant endo-type alginate lyase (Alg7D) from Saccharophagus degradans
Biotechnol. Lett.
34
1087-1092
2012
Saccharophagus degradans
EXTERNAL LINKS (specific for EC-Number 4.2.2.11)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
