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4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-2-O-sulfonato-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-2-O-sulfonato-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhyd
4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-2-O-sulfonato-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-2-O-sulfonato-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhyd
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4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-2-O-sulfonato-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-2-O-sulfonato-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhyd
inverting mechanism for the degradation of carrageenan by iota-carrageenases via single displacement reactions, overview
4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-2-O-sulfonato-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-2-O-sulfonato-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhyd
the enzyme hydrolyses the beta-(1->4) linkages in iota-carrageenans to produce a series of homologous, even-numbered oligosaccharides. The cleavage of glycosidic linkage catalyzed by iota-carrageenases also involves carboxylic acid-containing amino acid residues but, in contrast to kappa-carrageenases, it occurs via a direct, single displacement reaction by a water molecule, so that the configuration in the anomeric position is inverted
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4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-2-O-sulfonato-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-2-O-sulfonato-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhyd
the enzyme hydrolyses the beta-(1->4) linkages in iota-carrageenans to produce a series of homologous, even-numbered oligosaccharides. The cleavage of glycosidic linkage catalyzed by iota-carrageenases also involves carboxylic acid-containing amino acid residues but, in contrast to kappa-carrageenases, it occurs via a direct, single displacement reaction by a water molecule, so that the configuration in the anomeric position is inverted
4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-2-O-sulfonato-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-2-O-sulfonato-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhyd
the enzyme hydrolyses the beta-(1->4) linkages in iota-carrageenans to produce a series of homologous, even-numbered oligosaccharides. The cleavage of glycosidic linkage catalyzed by iota-carrageenases also involves carboxylic acid-containing amino acid residues but, in contrast to kappa-carrageenases, it occurs via a direct, single displacement reaction by a water molecule, so that the configuration in the anomeric position is inverted
4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-2-O-sulfonato-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhydro-2-O-sulfonato-alpha-D-galactopyranosyl-(1-3)-4-O-sulfonato-beta-D-galactopyranosyl-(1-4)-3,6-anhyd
the enzyme hydrolyses the beta-(1->4) linkages in iota-carrageenans to produce a series of homologous, even-numbered oligosaccharides. The cleavage of glycosidic linkage catalyzed by iota-carrageenases also involves carboxylic acid-containing amino acid residues but, in contrast to kappa-carrageenases, it occurs via a direct, single displacement reaction by a water molecule, so that the configuration in the anomeric position is inverted
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iota-/nu-carrageenan + H2O
hydrolyzed iota/nu-carrageenan
Alteromonas fortis
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the smallest hybrid is an octasaccharide with a iota-iota-nu-iota structure, the second fraction is composed of two decasaccharides with iota-iota-iota-nu-iota and iota-[iota/nu]iota-iota structures, the third fraction is a mixture of dodecasaccharides which contains at least a iota-iota-iota-iota-nu-iota oligosaccharide
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iota-carrageenan + H2O
hydrolyzed iota-carrageenan
iota-carrageenan + H2O
iota-carrabiose + iota-carratetraose
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?
iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose
iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose + iota-carrabiose
iota-carrageenan + H2O
iota-carratetraose
iota-carrageenan + H2O
iota-carratetraose + iota-carrabiose
iota-carrageenan + H2O
iota-neocarratetraose sulfate + iota-neocarrahexaose sulfate
iota-carrageenan + H2O
neo-iota-carratetraose
iota-carrageenan + H2O
neo-iota-carratetraose + ?
CgiF is an endo-type iota-carrageenase that hydrolyzes beta-1,4-linkages of iota-carrageenan, yielding neo-iota-carratetraose as the main product
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iota-carrageenan + H2O
neo-iota-carratetraose + neo-iota-carrahexaose
Alteromonas fortis
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most abundant products
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additional information
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iota-carrageenan + H2O
?
Alteromonas fortis
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iota-carrageenan + H2O
?
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iota-carrageenan + H2O
?
product is NI4
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iota-carrageenan + H2O
?
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iota-carrageenan + H2O
?
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iota-carrageenan + H2O
?
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iota-carrageenan + H2O
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iota-carrageenan + H2O
?
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iota-carrageenan + H2O
?
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iota-carrageenan + H2O
?
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iota-carrageenan + H2O
?
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iota-carrageenan + H2O
?
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iota-carrageenan + H2O
?
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iota-carrageenan + H2O
hydrolyzed iota-carrageenan
Alteromonas fortis
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?
iota-carrageenan + H2O
hydrolyzed iota-carrageenan
Alteromonas fortis
from an open conformation which allows the initial endo-attack of iota-carrageenan chains, the enzyme switches to a closed-tunnel form, consistent with its highly processive character
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?
iota-carrageenan + H2O
hydrolyzed iota-carrageenan
Alteromonas fortis
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hybrid kappa/iota-carrageeans extracted from Gigartina skottsbergii, Chondracanthus chamissoi, and Chondrus crispus are incubated with Pseudoalteromonas carrageenovora kappa-carrageenase and Alteromonas fortis iota-carrageenase. A low percentage of degradation is observed after treatment by iota-carrageenase, suggesting that long segments of iota-carrabiose or block of iota-carrageenan are low in abundance
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iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose
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?
iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose
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?
iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose
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?
iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose
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?
iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose
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?
iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose
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?
iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose
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iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose + iota-carrabiose
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iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose + iota-carrabiose
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?
iota-carrageenan + H2O
iota-carratetraose
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?
iota-carrageenan + H2O
iota-carratetraose
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?
iota-carrageenan + H2O
iota-carratetraose + iota-carrabiose
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?
iota-carrageenan + H2O
iota-carratetraose + iota-carrabiose
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iota-carrageenan + H2O
iota-carratetraose + iota-carrabiose
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disaccharides and tetrasaccharides as main products
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iota-carrageenan + H2O
iota-carratetraose + iota-carrabiose
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iota-carrageenan + H2O
iota-carratetraose + iota-carrabiose
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disaccharides and tetrasaccharides as main products
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?
iota-carrageenan + H2O
iota-carratetraose + iota-carrabiose
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iota-carrageenan + H2O
iota-carratetraose + iota-carrabiose
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disaccharides and tetrasaccharides as main products
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?
iota-carrageenan + H2O
iota-carratetraose + iota-carrabiose
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iota-carrageenan + H2O
iota-carratetraose + iota-carrabiose
commercial substrate type II, the major end product is iota-carrageenan tetrasaccharide, hydrolytic pattern analysis by mass spectrometry
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?
iota-carrageenan + H2O
iota-carratetraose + iota-carrabiose
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?
iota-carrageenan + H2O
iota-carratetraose + iota-carrabiose
commercial substrate type II, the major end product is iota-carrageenan tetrasaccharide, hydrolytic pattern analysis by mass spectrometry
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?
iota-carrageenan + H2O
iota-neocarratetraose sulfate + iota-neocarrahexaose sulfate
Alteromonas fortis
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?
iota-carrageenan + H2O
iota-neocarratetraose sulfate + iota-neocarrahexaose sulfate
the enzyme cleaves beta-1,4 linkages in iota-carrageenan to produce a high ratio of iota-carrageenan tetramer, more than 75% of the total product
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?
iota-carrageenan + H2O
iota-neocarratetraose sulfate + iota-neocarrahexaose sulfate
the enzyme cleaves beta-1,4 linkages in iota-carrageenan to produce a high ratio of iota-carrageenan tetramer, more than 75% of the total product
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?
iota-carrageenan + H2O
iota-neocarratetraose sulfate + iota-neocarrahexaose sulfate
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endohydrolytic cleavage, the enzyme proceeds with an overall inversion of the anomeric configuration
major end products
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?
iota-carrageenan + H2O
neo-iota-carratetraose
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iota-carrageenan + H2O
neo-iota-carratetraose
yielding neo-iota-carratetraose as the main product in the absence of NaCl
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?
iota-carrageenan + H2O
neo-iota-carratetraose
the endo-type iota-carrageenase hydrolyzes beta-1,4-linkages of iota-carrageenan
neo-carratetraose is the main product with more than 80% of the total product
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iota-carrageenan + H2O
neo-iota-carratetraose
the endo-type iota-carrageenase hydrolyzes beta-1,4-linkages of iota-carrageenan yielding neo-iota-carratetraose as the main product in the absence of NaCl, mass and NMR spectrometric product analysis, overview
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?
additional information
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no activity towards jota-carrageenan, kappa-carrageenan or agarose
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?
additional information
?
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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. iota-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
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?
additional information
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the enzyme does not cleave the beta-1,4 linkages in kappa- or lambda-carrageenan
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?
additional information
?
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the enzyme does not cleave the beta-1,4 linkages in kappa- or lambda-carrageenan
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?
additional information
?
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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. iota-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
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?
additional information
?
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analysis of hydrolysis products by thin layer chromatography, the endohydrolytic activity produces low molecular weight iota-carrageenan oligomers. The oligosaccharides observed include iota-carrageenan disaccharide (Dp2), tetrasaccharide (Dp4), and hexasaccharide (Dp6)
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?
additional information
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analysis of hydrolysis products by thin layer chromatography, the endohydrolytic activity produces low molecular weight iota-carrageenan oligomers. The oligosaccharides observed include iota-carrageenan disaccharide (Dp2), tetrasaccharide (Dp4), and hexasaccharide (Dp6)
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?
additional information
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the enzyme does not cleave the beta-1,4 linkages in kappa- or lambda-carrageenan
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?
additional information
?
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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. iota-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
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?
additional information
?
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the supernatant of marine bacterium Pseudoalteromonas carrageenovora ASY5 can degrade iota-carrageenans and kappa-carrageenans (EC 3.2.1.83)
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?
additional information
?
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analysis of hydrolysis products by ESI-mass spectrometry
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?
additional information
?
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the supernatant of marine bacterium Pseudoalteromonas carrageenovora ASY5 can degrade iota-carrageenans and kappa-carrageenans (EC 3.2.1.83)
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?
additional information
?
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analysis of hydrolysis products by ESI-mass spectrometry
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?
additional information
?
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the supernatant of marine bacterium Pseudoalteromonas carrageenovora ASY5 can degrade iota-carrageenans and kappa-carrageenans (EC 3.2.1.83)
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?
additional information
?
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analysis of hydrolysis products by ESI-mass spectrometry
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?
additional information
?
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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. iota-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
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?
additional information
?
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the recombinant enzyme exhibits slight effects on kappa-carrageenan (0.27 U/mg) and lambda-carrageenan (0.52 U/mg), those activities are two orders lower than that on iota-carrageenan, and may be attributed to the iota-carrageenan impurity in kappa-carrageenan and lambda-carrageenan substrates
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additional information
?
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the recombinant enzyme exhibits slight effects on kappa-carrageenan (0.27 U/mg) and lambda-carrageenan (0.52 U/mg), those activities are two orders lower than that on iota-carrageenan, and may be attributed to the iota-carrageenan impurity in kappa-carrageenan and lambda-carrageenan substrates
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additional information
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the recombinant enzyme exhibits slight effects on kappa-carrageenan (0.27 U/mg) and lambda-carrageenan (0.52 U/mg), those activities are two orders lower than that on iota-carrageenan, and may be attributed to the iota-carrageenan impurity in kappa-carrageenan and lambda-carrageenan substrates
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?
additional information
?
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the enzyme shows no activity with kappa-carrageenan, lambda-carrageenan, agar or agarose
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
iota-carrageenan + H2O
hydrolyzed iota-carrageenan
Alteromonas fortis
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?
iota-carrageenan + H2O
iota-carrabiose + iota-carratetraose
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?
iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose
iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose + iota-carrabiose
iota-carrageenan + H2O
iota-carratetraose
iota-carrageenan + H2O
iota-carratetraose + iota-carrabiose
iota-carrageenan + H2O
neo-iota-carratetraose
additional information
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iota-carrageenan + H2O
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iota-carrageenan + H2O
?
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iota-carrageenan + H2O
?
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iota-carrageenan + H2O
?
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iota-carrageenan + H2O
?
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iota-carrageenan + H2O
?
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iota-carrageenan + H2O
?
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iota-carrageenan + H2O
?
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iota-carrageenan + H2O
?
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iota-carrageenan + H2O
?
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iota-carrageenan + H2O
?
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iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose
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?
iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose
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?
iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose
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?
iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose
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?
iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose
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?
iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose
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?
iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose
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?
iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose + iota-carrabiose
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?
iota-carrageenan + H2O
iota-carrahexaose + iota-carratetraose + iota-carrabiose
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?
iota-carrageenan + H2O
iota-carratetraose
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?
iota-carrageenan + H2O
iota-carratetraose
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?
iota-carrageenan + H2O
iota-carratetraose + iota-carrabiose
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?
iota-carrageenan + H2O
iota-carratetraose + iota-carrabiose
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?
iota-carrageenan + H2O
iota-carratetraose + iota-carrabiose
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?
iota-carrageenan + H2O
iota-carratetraose + iota-carrabiose
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iota-carrageenan + H2O
iota-carratetraose + iota-carrabiose
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?
iota-carrageenan + H2O
iota-carratetraose + iota-carrabiose
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?
iota-carrageenan + H2O
neo-iota-carratetraose
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?
iota-carrageenan + H2O
neo-iota-carratetraose
yielding neo-iota-carratetraose as the main product in the absence of NaCl
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?
additional information
?
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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. iota-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
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?
additional information
?
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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. iota-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
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?
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. iota-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
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?
additional information
?
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the supernatant of marine bacterium Pseudoalteromonas carrageenovora ASY5 can degrade iota-carrageenans and kappa-carrageenans (EC 3.2.1.83)
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?
additional information
?
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the supernatant of marine bacterium Pseudoalteromonas carrageenovora ASY5 can degrade iota-carrageenans and kappa-carrageenans (EC 3.2.1.83)
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-
?
additional information
?
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the supernatant of marine bacterium Pseudoalteromonas carrageenovora ASY5 can degrade iota-carrageenans and kappa-carrageenans (EC 3.2.1.83)
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?
additional information
?
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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. iota-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
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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physiological function
iota-carrageenases play a role in marine iota-carrageenan degradation, and their enzymatic hydrolysatesare thought to be excellent antioxidants
additional information
residues R243, R303, and R353 are involved in substrate binding, residues E245, D247, E310, and H281 are catalytic residues. Glu245 acts as a catalytic proton donor in CgiA, and Asp247 acts as the general base that activates the catalytic water molecule. Three other residues are indirectly involved in the activity: Gln222 simultaneously binds the catalytic water molecule and a chloride ion, playing the essential function of structuring the water network in the active site. His281 participates in iota-carrageenan binding and is likely involved in proton trafficking with the proton donor Glu245, and Glu310 stabilizes the substrate intermediate conformation. Active site structure and molecular docking, overview
evolution
the enzyme belongs to glycohydrolase family 82, GH82, forming a deeply branched cluster in the phylogenetic tree, along with Celly_2571 and CgiA3, distinct from other iota-carrageenases
evolution
the enzyme belongs to the glycosyl hydrolase family 82, GH82
evolution
the enzyme belongs to the glycosyl hydrolase family 82, GH82
evolution
-
the enzyme belongs to the glycoside hydrolases family 82, GH 82. 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
evolution
the enzyme belongs to the glycoside hydrolases family 82, GH 82. 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
evolution
the enzyme belongs to the glycoside hydrolases family 82, GH 82. 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
evolution
the enzyme belongs to the glycosyl hydrolase family 82, GH82, phylogenetic analysis of carrageenases from different groups, overview
evolution
the enzyme belongs to the glycosyl hydrolase family 82, GH82, phylogenetic analysis of carrageenases from different groups, overview
evolution
the enzyme belongs to the glycosyl hydrolase family 82, GH82, phylogenetic analysis of carrageenases from different groups, overview
evolution
the enzyme belongs to the glycosyl hydrolase family 82, GH82, phylogenetic analysis of carrageenases from different groups, overview
evolution
the enzyme belongs to the glycosyl hydrolase family 82, GH82, phylogenetic analysis of carrageenases from different groups, overview
evolution
the enzyme belongs to the glycosyl hydrolase family 82, GH82, phylogenetic analysis of carrageenases from different groups, overview
evolution
-
the enzyme belongs to the glycosyl hydrolase family 82, GH82, phylogenetic analysis of carrageenases from different groups, overview
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 82, GH82, phylogenetic analysis of carrageenases from different groups, overview
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 82, GH82, phylogenetic analysis of carrageenases from different groups, overview
-
evolution
-
the enzyme belongs to the glycoside hydrolases family 82, GH 82. 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
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 82, GH82, phylogenetic analysis of carrageenases from different groups, overview
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 82, GH82, phylogenetic analysis of carrageenases from different groups, overview
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 82, GH82, phylogenetic analysis of carrageenases from different groups, overview
-
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
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
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
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
-
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expressed in Bacillus subtilis
expressed in Escherichia coli BL21(DE3) cells
Alteromonas fortis
-
expressed in Escherichia coli Origami (DE3) pLysS, BL21 (DE3), C41 (DE3), and C43 (DE3) cells
Alteromonas fortis
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gene cgi82A, recombinant expression of His6-tagged enzyme in Escherichia coli
gene cgiA, sequence comparisons and phylogenetic analysis
gene cgiA2, sequence comparisons and phylogenetic analysis
gene cgiB, sequence comparisons and phylogenetic analysis
gene cgiB_Ce, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli strain BL21(DE3)
gene cgiB_Ce, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene cgiF, sequence comparisons and phylogenetic analysis
gene cgiF, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
gene encoding iota-carrageenase flanked by a C-terminal hexahistidine tag and a N-terminal PelB signal peptide for targeting the gene product into Escherichia coli periplasm. The recombinant plasmid, referred to as pETIAf, is used to transform Escherichia coli BL21(DE3) strain harbouring pLysS plasmid
Alteromonas fortis
-
overexpressed in Escherichia coli BL21(DE3)
Alteromonas fortis
-
synthetic gene CGIOP, locus MF459059 in GenBank, codon-optimized gene encoding the iota-carrageenase without a signal peptide, cloned from gene cgiA of Microbulbifer thermotolerans strain JAMB-A94, construction of the integrative vector pBCGA, recombinant expression of extracellular His-tagged enzyme in Brevibacillus choshinensis strain HPD31-SP3, real-time PCR expression analysis, copy numbers of the CGIOP gene in different lines are approximately 5-6, respectively
gene cgiA, sequence comparisons and phylogenetic analysis
gene cgiA, sequence comparisons and phylogenetic analysis
gene cgiA, sequence comparisons and phylogenetic analysis
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Michel, G.; Flament, D.; Barbeyron, T.; Vernet, T.; Kloareg, B.; Dideberg, O.
Expression, purification, crystallization and preliminary X-ray analysis of the iota-carrageenase from Alteromonas fortis
Acta Crystallogr. Sect. D
56
766-768
2000
Alteromonas fortis
brenda
Barbeyron, T.; Michel, G.; Potin, P.; Henrissat, B.; Kloareg, B.
iota-Carrageenases constitute a novel family of glycoside hydrolases, unrelated to that of kappa-carrageenases
J. Biol. Chem.
275
35499-35505
2000
Zobellia galactanivorans
brenda
Michel, G.; Chantalat, L.; Fanchon, E.; Henrissat, B.; Kloareg, B.; Dideberg, O.
The iota-carrageenase of Alteromonas fortis. A beta-helix fold-containing enzyme for the degradation of a highly polyanionic polysaccharide
J. Biol. Chem.
276
40202-40209
2001
Alteromonas fortis
brenda
Michel, G.; Helbert, W.; Kahn, R.; Dideberg, O.; Kloareg, B.
The structural bases of the processive degradation of iota-carrageenan, a main cell wall polysaccharide of red algae
J. Mol. Biol.
334
421-433
2003
Alteromonas fortis (Q9F5I8)
brenda
Mennink-Kersten, M.A.; Ruegebrink, D.; Wasei, N.; Melchers, W.J.; Verweij, P.E.
In vitro release by Aspergillus fumigatus of galactofuranose antigens, 1,3-beta-D-glucan, and DNA, surrogate markers used for diagnosis of invasive aspergillosis
J. Clin. Microbiol.
44
1711-1718
2006
Alteromonas fortis
brenda
Jouanneau, D.; Boulenguer, P.; Mazoyer, J.; Helbert, W.
Complete assignment of 1H and 13C NMR spectra of standard neo-iota-carrabiose oligosaccharides
Carbohydr. Res.
345
547-551
2010
Alteromonas fortis
brenda
Jouanneau, D.; Boulenguer, P.; Mazoyer, J.; Helbert, W.
Enzymatic degradation of hybrid iota-/nu-carrageenan by Alteromonas fortis iota-carrageenase
Carbohydr. Res.
345
934-940
2010
Alteromonas fortis
brenda
Rebuffet, E.; Barbeyron, T.; Jeudy, A.; Jam, M.; Czjzek, M.; Michel, G.
Identification of catalytic residues and mechanistic analysis of family GH82 iota-carrageenases
Biochemistry
49
7590-7599
2010
Alteromonas fortis
brenda
Hatada, Y.; Mizuno, M.; Li, Z.; Ohta, Y.
Hyper-production and characterization of the iota-carrageenase useful for iota-carrageenan oligosaccharide production from a deep-sea bacterium, Microbulbifer thermotolerans JAMB-A94T, and insight into the unusual catalytic mechanism
Mar. Biotechnol.
13
411-422
2011
Microbulbifer thermotolerans (E3W9G3), Microbulbifer thermotolerans, Microbulbifer thermotolerans JAMB-A94T (E3W9G3)
brenda
Ma, S.; Tan, Y.L.; Yu, W.G.; Han, F.
Cloning, expression and characterization of a new iota-carrageenase from marine bacterium, Cellulophaga sp.
Biotechnol. Lett.
35
1617-1622
2013
Cellulophaga sp. (R9UQG9)
brenda
Prechoux, A.; Genicot, S.; Rogniaux, H.; Helbert, W.
Controlling carrageenan structure using a novel formylglycine-dependent sulfatase, an endo-4S-iota-carrageenan sulfatase
Mar. Biotechnol.
15
265-274
2013
Alteromonas fortis
brenda
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
Wenyingzhuangia fucanilytica (A0A1B1Y261), Flavobacterium sp. YS-80-122 (A0A1W5QBK3), Zobellia galactanivorans (D9UAT1), Zobellia galactanivorans (Q9F284), Microbulbifer thermotolerans (E3W9G3), Alteromonas macleodii (Q9F5I8), Cellulophaga sp. QY3 (R9UQG9), Zobellia galactanivorans CCUG 47099 (D9UAT1), Zobellia galactanivorans CCUG 47099 (Q9F284), Zobellia galactanivorans Dsij (D9UAT1), Zobellia galactanivorans Dsij (Q9F284), Zobellia galactanivorans DSM 12802 (D9UAT1), Zobellia galactanivorans DSM 12802 (Q9F284), Zobellia galactanivorans CIP 106680 (D9UAT1), Zobellia galactanivorans CIP 106680 (Q9F284), Microbulbifer thermotolerans JAMB-A94T (E3W9G3), Zobellia galactanivorans NCIMB 13871 (D9UAT1), Zobellia galactanivorans NCIMB 13871 (Q9F284)
brenda
Xiao, Q.; Zhu, Y.; Li, J.; Wu, C.; Ni, H.; Xiao, A.
Fermentation optimization and enzyme characterization of a new iota-carrageenase from Pseudoalteromonas carrageenovora ASY5
Electron. J. Biotechnol.
32
26-34
2018
Pseudoalteromonas carrageenovora, Pseudoalteromonas carrageenovora CICC 23819, Pseudoalteromonas carrageenovora ASY5
-
brenda
Li, S.; Hao, J.; Sun, M.
Cloning and characterization of a new cold-adapted and thermo-tolerant iota-carrageenase from marine bacterium Flavobacterium sp. YS-80-122
Int. J. Biol. Macromol.
102
1059-1065
2017
Flavobacterium sp. YS-80-122 (A0A1W5QBK3)
brenda
Shen, J.; Chang, Y.; Dong, S.; Chen, F.
Cloning, expression and characterization of a iota-carrageenase from marine bacterium Wenyingzhuangia fucanilytica A biocatalyst for producing iota-carrageenan oligosaccharides
J. Biotechnol.
259
103-109
2017
Wenyingzhuangia fucanilytica (A0A1B1Y261), Wenyingzhuangia fucanilytica, Wenyingzhuangia fucanilytica CZ1127 (A0A1B1Y261)
brenda
Ghanbarzadeh, M.; Golmoradizadeh, A.; Homaei, A.
Carrageenans and carrageenases versatile polysaccharides and promising marine enzymes
Phytochem. Rev.
17
535-571
2018
uncultured bacterium, Microbulbifer thermotolerans (E3W9G3), Cellulophaga sp. QY3 (R9UQG9), Microbulbifer thermotolerans JAMBA94T (E3W9G3)
-
brenda
Xu, Y.; Mao, W.; Gao, W.; Chi, Z.; Chi, Z.; Liu, G.
Efficient production of a recombinant iota-carrageenase in Brevibacillus choshinensis using a new integrative vector for the preparation of iota-carrageenan oligosaccharides
Process Biochem.
76
68-76
2019
Microbulbifer thermotolerans (E3W9G3), Microbulbifer thermotolerans JAMB-A94 (E3W9G3)
-
brenda