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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.
3.2.1.157 iota-carrageenase
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