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Information on EC 3.2.1.162 - lambda-carrageenase and Organism(s) Pseudoalteromonas carrageenovora and UniProt Accession Q0JRK4

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Pseudoalteromonas carrageenovora
UNIPROT: Q0JRK4 not found.
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The taxonomic range for the selected organisms is: Pseudoalteromonas carrageenovora
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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Endohydrolysis of (1->4)-beta-linkages in the backbone of lambda-carrageenan, resulting in the tetrasaccharide alpha-D-Gal-p2,6S2-(1->3)-beta-D-Gal-p2S-(1->4)-alpha-D-Gal-p2,6S2-(1->3)-D-Gal-p2-S
Synonyms
lambda-carrageenase, cga-l50, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Endohydrolysis of (1->4)-beta-linkages in the backbone of lambda-carrageenan, resulting in the tetrasaccharide alpha-D-Gal-p2,6S2-(1->3)-beta-D-Gal-p2S-(1->4)-alpha-D-Gal-p2,6S2-(1->3)-D-Gal-p2-S
show the reaction diagram
proceeds according to an endolytic mode of action and a mechanism of inversion of the anomeric configuration
PATHWAY SOURCE
PATHWAYS
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
50936-37-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
lambda-carrageenan + H2O
?
show the reaction diagram
lambda-carrageenan + H2O
neo-lambda-carratetraose + neo-lambda-carrahexaose
show the reaction diagram
CglA hydrolase proceeds according to an endolytic mode of action and a mechanism of inversion of the anomeric configuration
neo-lambda-carratetraose is the main degradation product
-
?
lambda-carrageenan + H2O
neo-carrabiose oligosaccharides
show the reaction diagram
-
-
-
-
?
lambda-carrageenan + H2O
neo-lambda-carratetraose + neo-lambda-carrahexaose
show the reaction diagram
neo-lambda-carrahexaose + H2O
neo-lambda-carratetraose + neo-lambda-carrabiose
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
lambda-carrageenan + H2O
?
show the reaction diagram
-
-
-
?
lambda-carrageenan + H2O
neo-lambda-carratetraose + neo-lambda-carrahexaose
show the reaction diagram
sole known depolymerizing enzyme of lambda-carrageenan, hydrolyses the beta(1-4) linkage of lambda-carrageenan
main reaction products
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
phylogenetic analysis of carrageenases from different groups, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CGLA_PSEVC
942
0
105638
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
97000
1 * 97000, SDS-PAGE
105000
pre-protein, calculated from the deduced amino acid sequence
109000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 97000, SDS-PAGE
?
-
x * 109000, His-tagged enzyme, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
generation of a chimeric protein cCgkA and cCglA containing the catalytic domain of kappa-carrageenase CgkA and delta-carrageenase CglA fused with a dockerin domain, miniCbpA, cCgkA and cCglA assemble into a complex, the dockerin-fused enzymes on the scaffoldin have synergistic activity in the degradationof carrageenan showing enhancement of activity by carrageenolytic complex 3.1fold higher compared with the corresponding enzymes alone
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, recombinant chimeric protein cCgkA and cCglA containing the catalytic domain of kappa-carrageenase CgkA and delta-carrageenase CglA fused with a dockerin domain from Escherichia coli strain BL21(DE3) by cellulose affinity chromatography using carbohydrate binding module in scaffoldin miniCbpA as a tag
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli as insoluble inclusion bodies. These inclusion bodies are purified and solubilized in 8 M urea
gene cglA, phylogenetic analysis, overview
expressed as His-tag fusion protein in Escherichia coli, formation of inclusion bodies that are solved in 8 M urea
subcloning in Escherichia coli strain DH5alpha, recombinant expression of a chimeric protein cCgkA and cCglA containing the catalytic domain of kappa-carrageenase CgkA and delta-carrageenase CglA fused with a dockerin domain in Escherichia coli strain BL21(DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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the assemblies of advancement of active enzyme complexes, i.e. of kappa-carrageenase CgkA and delta-carrageenase CglA, will facilitate the commercial production of useful products from red algae biomass whichrepresents inexpensive and sustainable feed-stocks
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Guibet, M.; Colin, S.; Barbeyron, T.; Genicot, S.; Kloareg, B.; Michel, G.; Helbert, W.
Degradation of lambda-carrageenan by Pseudoalteromonas carrageenovora lambda-carrageenase: a new family of glycoside hydrolases unrelated to kappa- and iota-carrageenases
Biochem. J.
404
105-114
2007
Pseudoalteromonas carrageenovora, Pseudoalteromonas carrageenovora (Q0JRK4), Pseudoalteromonas carrageenovora ATCC 43555
Manually annotated by BRENDA team
Guibet, M.; Kervarec, N.; Genicot, S.; Chevolot, Y.; Helbert, W.
Complete assignment of 1H and 13C NMR spectra of Gigartina skottsbergii lambda-carrageenan using carrabiose oligosaccharides prepared by enzymatic hydrolysis
Carbohydr. Res.
341
1859-1869
2006
Pseudoalteromonas carrageenovora
Manually annotated by BRENDA team
Kang, D.H.; Hyeon, J.E.; You, S.K.; Kim, S.W.; Han, S.O.
Efficient enzymatic degradation process for hydrolysis activity of the carrageenan from red algae in marine biomass
J. Biotechnol.
192 Pt A
108-113
2014
Pseudoalteromonas carrageenovora
Manually annotated by BRENDA team
Zhu, B.; Ni, F.; Sun, Y.; Zhu, X.; Yin, H.; Yao, Z.; Du, Y.
Insight into carrageenases major review of sources, category, property, purification method, structure, and applications
Crit. Rev. Biotechnol.
38
1261-1276
2018
Pseudoalteromonas carrageenovora (Q0JRK4), Pseudoalteromonas sp. CL19 (Q05JY7)
Manually annotated by BRENDA team