BRENDA - Enzyme Database
show all sequences of 3.2.1.162

Carrageenans and carrageenases versatile polysaccharides and promising marine enzymes

Ghanbarzadeh, M.; Golmoradizadeh, A.; Homaei, A.; Phytochem. Rev. 17, 535-571 (2018)
No PubMed abstract available

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
lambda-carrageenan + H2O
Bacillus sp. Lc50-1
-
?
-
-
?
additional information
Bacillus sp. Lc50-1
kappa-, iota- and lambda-carrageenase display strict specificity for their substrates, namely kappa-, iota- and lambda-carrageenans, respectively. The enzymes discriminate the substrate probably by recognizing the sulfation pattern of the digalactose reapeting unit of the polysaccharide. lambda-Carrageenas present conserved arginine residues in the catalytic site which are believed to interact with carrageenans in which both sugar residues in the disaccharide units are negatively charged
?
-
-
-
Organism
Organism
UniProt
Commentary
Textmining
Bacillus sp. Lc50-1
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
native enzyme 37.8fold by gel filtration
Bacillus sp. Lc50-1
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
105.9
-
purified native enzyme, pH and temperature not specified in the publication
Bacillus sp. Lc50-1
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
lambda-carrageenan + H2O
-
755018
Bacillus sp. Lc50-1
?
-
-
-
?
additional information
kappa-, iota- and lambda-carrageenase display strict specificity for their substrates, namely kappa-, iota- and lambda-carrageenans, respectively. The enzymes discriminate the substrate probably by recognizing the sulfation pattern of the digalactose reapeting unit of the polysaccharide. lambda-Carrageenas present conserved arginine residues in the catalytic site which are believed to interact with carrageenans in which both sugar residues in the disaccharide units are negatively charged
755018
Bacillus sp. Lc50-1
?
-
-
-
-
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
75
-
purified enzyme, 45 min, 50% activity remaining
Bacillus sp. Lc50-1
85
-
purified enzyme, 10 min, 50% activity remaining
Bacillus sp. Lc50-1
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Bacillus sp. Lc50-1
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
6
9
purified enzyme, 15 min, 70% activity remaining
Bacillus sp. Lc50-1
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
lambda-carrageenan + H2O
Bacillus sp. Lc50-1
-
?
-
-
?
additional information
Bacillus sp. Lc50-1
kappa-, iota- and lambda-carrageenase display strict specificity for their substrates, namely kappa-, iota- and lambda-carrageenans, respectively. The enzymes discriminate the substrate probably by recognizing the sulfation pattern of the digalactose reapeting unit of the polysaccharide. lambda-Carrageenas present conserved arginine residues in the catalytic site which are believed to interact with carrageenans in which both sugar residues in the disaccharide units are negatively charged
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
native enzyme 37.8fold by gel filtration
Bacillus sp. Lc50-1
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
105.9
-
purified native enzyme, pH and temperature not specified in the publication
Bacillus sp. Lc50-1
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
lambda-carrageenan + H2O
-
755018
Bacillus sp. Lc50-1
?
-
-
-
?
additional information
kappa-, iota- and lambda-carrageenase display strict specificity for their substrates, namely kappa-, iota- and lambda-carrageenans, respectively. The enzymes discriminate the substrate probably by recognizing the sulfation pattern of the digalactose reapeting unit of the polysaccharide. lambda-Carrageenas present conserved arginine residues in the catalytic site which are believed to interact with carrageenans in which both sugar residues in the disaccharide units are negatively charged
755018
Bacillus sp. Lc50-1
?
-
-
-
-
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
75
-
purified enzyme, 45 min, 50% activity remaining
Bacillus sp. Lc50-1
85
-
purified enzyme, 10 min, 50% activity remaining
Bacillus sp. Lc50-1
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Bacillus sp. Lc50-1
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
6
9
purified enzyme, 15 min, 70% activity remaining
Bacillus sp. Lc50-1
General Information
General Information
Commentary
Organism
evolution
lambda-carrageenases belong to a to date unclassified GH family in the carbohydrateactive enzymes (CAZy) database. In spite of having specificities for structure-related substrates, kappa-, iota- and lambda-carrageenases do not share significant sequence homology, although all of them share some common binding site for ions important in stabilizing the enzyme
Bacillus sp. Lc50-1
metabolism
the most important types of commercial carrageenans, namely kappa-, iota- and lambda-carrageenan, are esterified with one, two, and three sulfate groups per repeating disaccharide unit, being also called carrageenose 4'-sulfate, carrageenose 2,4'-disulfate, and carrageenose 2,6,2'-trisulfate, respectively. kappa-Carrageenans occur in the cell wall of some species of marine red algae, such as Chondrus sp., Gigartina sp., Eucheuma sp. and Iridaea sp. but is mostly extracted from tropical seaweed Euchema cottoni (also known as Kappaphycus alvarezii), while iota-carrageenans are mainly extracted from Eucheuma spinosum (also known as Eucheuma denticulatum). Because kappa- and iota-carrageenans are produced from my- and ny-carrageenans, respectively, during the extraction under alkaline at high temperatures or biosynthetically by a reaction catalyzed by the enzyme sulfohydrolase, these polysaccharides are often found in commercial samples. lambda-Carrageenans are extracted from red algae within the Gigartina and Chondrus genera, which produces this type of polysaccharide during the sporophytic stage. These algae are also a source of kappa- and iota-carrageenans when they are in the gametophytic stage, but because they produce mixed chain polysaccharide chains containing both kappa- and iota-units, extraction of kappa- and iota-carrageenans from the mentioned algae is preferred. Carrageenan classes based on the number and position of sulfate groups in the chain, overview. The sulfate and AD contents of commercial kappa-, iota-, and lambda-carrageenans have been determined by acid hydrolysis, infrared spectroscopy, and nuclear magnetic resonance (NMR) analyses and found to be, respectively, 25-30 and 28-35% for the kappa-type, 28-30 and 25-30% for iota-type and 32-39% and 0 for lambda-type, respectively
Bacillus sp. Lc50-1
General Information (protein specific)
General Information
Commentary
Organism
evolution
lambda-carrageenases belong to a to date unclassified GH family in the carbohydrateactive enzymes (CAZy) database. In spite of having specificities for structure-related substrates, kappa-, iota- and lambda-carrageenases do not share significant sequence homology, although all of them share some common binding site for ions important in stabilizing the enzyme
Bacillus sp. Lc50-1
metabolism
the most important types of commercial carrageenans, namely kappa-, iota- and lambda-carrageenan, are esterified with one, two, and three sulfate groups per repeating disaccharide unit, being also called carrageenose 4'-sulfate, carrageenose 2,4'-disulfate, and carrageenose 2,6,2'-trisulfate, respectively. kappa-Carrageenans occur in the cell wall of some species of marine red algae, such as Chondrus sp., Gigartina sp., Eucheuma sp. and Iridaea sp. but is mostly extracted from tropical seaweed Euchema cottoni (also known as Kappaphycus alvarezii), while iota-carrageenans are mainly extracted from Eucheuma spinosum (also known as Eucheuma denticulatum). Because kappa- and iota-carrageenans are produced from my- and ny-carrageenans, respectively, during the extraction under alkaline at high temperatures or biosynthetically by a reaction catalyzed by the enzyme sulfohydrolase, these polysaccharides are often found in commercial samples. lambda-Carrageenans are extracted from red algae within the Gigartina and Chondrus genera, which produces this type of polysaccharide during the sporophytic stage. These algae are also a source of kappa- and iota-carrageenans when they are in the gametophytic stage, but because they produce mixed chain polysaccharide chains containing both kappa- and iota-units, extraction of kappa- and iota-carrageenans from the mentioned algae is preferred. Carrageenan classes based on the number and position of sulfate groups in the chain, overview. The sulfate and AD contents of commercial kappa-, iota-, and lambda-carrageenans have been determined by acid hydrolysis, infrared spectroscopy, and nuclear magnetic resonance (NMR) analyses and found to be, respectively, 25-30 and 28-35% for the kappa-type, 28-30 and 25-30% for iota-type and 32-39% and 0 for lambda-type, respectively
Bacillus sp. Lc50-1
Other publictions for EC 3.2.1.162
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
753336
Zhu
Insight into carrageenases ma ...
Pseudoalteromonas carrageenovora, Pseudoalteromonas sp. CL19
Crit. Rev. Biotechnol.
38
1261-1276
2018
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2
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4
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2
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2
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2
2
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755018
Ghanbarzadeh
-
Carrageenans and carrageenase ...
Bacillus sp. Lc50-1
Phytochem. Rev.
17
535-571
2018
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2
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1
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1
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1
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2
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731525
Li
Purification and characterizat ...
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) Lc50-1
Biotechnol. Lett.
36
1669-1674
2014
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7
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5
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1
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732212
Kang
Efficient enzymatic degradatio ...
Pseudoalteromonas carrageenovora
J. Biotechnol.
192 Pt A
108-113
2014
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1
1
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1
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667539
Guibet
Degradation of lambda-carragee ...
Pseudoalteromonas carrageenovora, Pseudoalteromonas carrageenovora ATCC 43555
Biochem. J.
404
105-114
2007
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1
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4
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7
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668168
Guibet
Complete assignment of 1H and ...
Pseudoalteromonas carrageenovora
Carbohydr. Res.
341
1859-1869
2006
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669161
Ohta
A novel enzyme, lambda-carrage ...
Pseudoalteromonas sp.
J. Biochem.
140
475-481
2006
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668129
Johnston
Enzymic hydrolysis of the pota ...
Pseudomonas carrageenovora
Can. J. Microbiol.
19
779-788
1973
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