Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2'-fucosyllactose + H2O
lactose + fucose
-
Fuc-alpha-(1->2)-Gal-beta-(1->4)-Glc
-
-
?
4-methylumbelliferyl 2-acetamido-2-deoxy-3-O-(beta-D-galactopyranosyl)-D-glucopyranoside + H2O
4-methylumbelliferol + 2-acetamido-2-deoxy-3-O-(beta-D-galactopyranosyl)-D-glucopyranose
-
-
-
?
4-nitrophenyl-beta-lacto-N-bioside + H2O
4-nitrophenol + lacto-N-biose
4-nitrophenyl-Gal-beta-(1->3)-GalNAc + H2O
4-nitrophenol + Gal-beta-(1->3)-GalNAc
4-nitrophenyl-GalNAc-beta-(1->3)-GlcNAc + H2O
4-nitrophenol + GalNAc-beta-(1->3)-GlcNAc
-
-
-
?
4-nitrophenyl-lacto-N-bioside + H2O
4-nitrophenol + lacto-N-biose
-
-
-
?
D-Gal-(1,3)-beta-GlcNAc-(1,3)-beta-D-Gal-(1,4)-beta-D-Glc-pyridylamine + H2O
?
lacto-N-tetraose-pyridylamine, no activity on alpha-linked disaccharides, beta-linked p-nitrophenyl monosaccharides such as 4-nitrophenyl beta-D-N-acetylglucosamine and 4-nitrophenyl beta-D-N-acetyl-D-galactosamine, no activity on ganglioside GA1 structure with beta-linked galacto-N-biose, no activity on fucosylated forms of lacto-N-tetraose or lacto-N-neotetraose
-
-
?
D-Gal-(1,3)-beta-GlcNAc-(1,3)-beta-D-Gal-(1,4)-D-Glc + H2O
lactose + D-galactosyl-beta-1,3-N-acetyl-D-glucosamine
Fuc-alpha-(1->2)-Gal-beta-(1->3)-GalNAc-beta-(1->3)-Gal-alpha-(1->4)-Gal-beta-(1->4)-Glc + H2O
Fuc-alpha-(1->2)-Gal-beta-(1->3)-GalNAc + Gal-alpha-(1->4)-Gal-beta-(1->4)-Glc
i.e. Globo H
-
-
?
Fuc-alpha-(1->2)-Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc + H2O
Fuc-alpha-(1->2)-Gal-beta-(1->3)-GlcNAc + Gal-beta-(1->4)-Glc
i.e. LNFP I
-
-
?
Gal-beta-(1->3)-GalNAc-beta-(1->3)-Gal-alpha-(1->4)-Gal-beta-(1->4)-Glc + H2O
Gal-beta-(1->3)-GalNAc + Gal-alpha-(1->4)-Gal-beta-(1->4)-Glc
Gal-beta-(1->3)-GalNAc-beta-(1->4)-Gal-beta-(1->4)-Glc + H2O
Gal-beta-(1->3)-GlcNAc + Gal-beta-(1->4)-Glc
i.e. GA1
-
-
?
Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc + H2O
Gal-beta-(1->3)-GlcNAc + Gal-beta-(1->4)-Glc
Galbeta1-3GlcNAcbeta-p-nitrophenol + H2O
Galbeta1-3GlcNAc + p-nitrophenol
Galbeta1-3GlcNAcbeta-p-nitrophenol + lactose
Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc + ?
Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc-pyridylamine + H2O
?
lacto-N-difucohexaose + H2O
lactose + Fuc-alpha-(1->2)-Gal-beta-(1->3)[Fuc-alpha-(1->4)]GlcNAc
-
Fuc-alpha-(1->2)Gal-beta-(1->3)[Fuc-alpha-(1->4)]GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc
-
-
?
lacto-N-fucopentaose I + H2O
lactose + Fuc-alpha-(1->2)-Gal-beta-(1->3)-GlcNAc
lacto-N-hexaose + H2O
lactose + lacto-N-tetraose
Gal-beta-(1->3)-GlcNAc-beta-(1->3)-[Gal-beta-(1->4)-GlcNAc-beta-(1->6)]-beta-(1->4)-Glc
-
-
?
lacto-N-tetraose + H2O
lacto-N-biose + lactose
lacto-N-tetraose + H2O
lacto-N-biose I + lactose
-
-
-
?
lacto-N-tetraose + H2O
lactose + lacto-N-biose
p-nitrophenyl-Gal-(1,3)-beta-GalNAc + H2O
?
30% enzyme activity compared to p-nitrophenyl-Gal-(1,3)-beta-GlcNAc
-
-
?
p-nitrophenyl-Gal-(1,3)-beta-GlcNAc + H2O
?
p-nitrophenyl-lacto-N-bioside + H2O
p-nitrophenol + lacto-N-biose
pyridylamine-oligosaccharides which have type 1 chains at the nonreducing terminus + H2O
lacto-N-biose + ?
sialyllacto-N-tetraose a + H2O
lactose + Fuc-alpha-(1->2)-Gal-beta-(1->3)[Fuc-alpha-(1->4)]GlcNAc
additional information
?
-
4-nitrophenyl-beta-lacto-N-bioside + H2O
4-nitrophenol + lacto-N-biose
-
-
-
?
4-nitrophenyl-beta-lacto-N-bioside + H2O
4-nitrophenol + lacto-N-biose
-
-
-
?
4-nitrophenyl-Gal-beta-(1->3)-GalNAc + H2O
4-nitrophenol + Gal-beta-(1->3)-GalNAc
-
-
-
?
4-nitrophenyl-Gal-beta-(1->3)-GalNAc + H2O
4-nitrophenol + Gal-beta-(1->3)-GalNAc
-
-
-
?
D-Gal-(1,3)-beta-GlcNAc-(1,3)-beta-D-Gal-(1,4)-D-Glc + H2O
lactose + D-galactosyl-beta-1,3-N-acetyl-D-glucosamine
lacto-N-tetraose, major component of human milk oligosaccharides
lacto-N-biose I
-
?
D-Gal-(1,3)-beta-GlcNAc-(1,3)-beta-D-Gal-(1,4)-D-Glc + H2O
lactose + D-galactosyl-beta-1,3-N-acetyl-D-glucosamine
-
lacto-N-tetraose, major component of human milk oligosaccharides
lacto-N-biose I
-
?
Gal-beta-(1->3)-GalNAc-beta-(1->3)-Gal-alpha-(1->4)-Gal-beta-(1->4)-Glc + H2O
Gal-beta-(1->3)-GalNAc + Gal-alpha-(1->4)-Gal-beta-(1->4)-Glc
i.e. Gb5
-
-
?
Gal-beta-(1->3)-GalNAc-beta-(1->3)-Gal-alpha-(1->4)-Gal-beta-(1->4)-Glc + H2O
Gal-beta-(1->3)-GalNAc + Gal-alpha-(1->4)-Gal-beta-(1->4)-Glc
i.e. Gb5
-
-
?
Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc + H2O
Gal-beta-(1->3)-GlcNAc + Gal-beta-(1->4)-Glc
i.e. LNT
-
-
?
Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc + H2O
Gal-beta-(1->3)-GlcNAc + Gal-beta-(1->4)-Glc
i.e. LNT
-
-
?
Galbeta1-3GlcNAcbeta-p-nitrophenol + H2O
Galbeta1-3GlcNAc + p-nitrophenol
-
-
-
-
?
Galbeta1-3GlcNAcbeta-p-nitrophenol + H2O
Galbeta1-3GlcNAc + p-nitrophenol
-
-
-
-
?
Galbeta1-3GlcNAcbeta-p-nitrophenol + lactose
Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc + ?
-
-
Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc, i.e. lacto-neotetraose
-
?
Galbeta1-3GlcNAcbeta-p-nitrophenol + lactose
Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc + ?
-
-
Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc, i.e. lacto-neotetraose
-
?
Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc-pyridylamine + H2O
?
-
-
-
-
?
Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc-pyridylamine + H2O
?
-
-
-
-
?
lacto-N-fucopentaose I + H2O
lactose + Fuc-alpha-(1->2)-Gal-beta-(1->3)-GlcNAc
-
Fuc-alpha-(1->2)-Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc
-
-
?
lacto-N-fucopentaose I + H2O
lactose + Fuc-alpha-(1->2)-Gal-beta-(1->3)-GlcNAc
Fuc-alpha-(1->2)-Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc
-
-
?
lacto-N-fucopentaose I + H2O
lactose + Fuc-alpha-(1->2)-Gal-beta-(1->3)-GlcNAc
Fuc-alpha-(1->2)-Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc
-
-
?
lacto-N-tetraose + H2O
lacto-N-biose + lactose
-
-
-
?
lacto-N-tetraose + H2O
lacto-N-biose + lactose
-
-
-
-
?
lacto-N-tetraose + H2O
lactose + lacto-N-biose
-
Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc
-
-
?
lacto-N-tetraose + H2O
lactose + lacto-N-biose
-
lacto-N-tetraose is a major component of human milk oligosaccharides, substrate used to examine the LnbB activities in various bacterial strains
-
-
?
lacto-N-tetraose + H2O
lactose + lacto-N-biose
-
lacto-N-tetraose is a major component of human milk oligosaccharides, substrate used to examine the LnbB activities in various bacterial strains
-
-
?
lacto-N-tetraose + H2O
lactose + lacto-N-biose
Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc
-
-
?
lacto-N-tetraose + H2O
lactose + lacto-N-biose
Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc
-
-
?
lacto-N-tetraose + H2O
lactose + lacto-N-biose
-
-
-
-
?
lacto-N-tetraose + H2O
lactose + lacto-N-biose
-
-
-
-
?
p-nitrophenyl-Gal-(1,3)-beta-GlcNAc + H2O
?
lacto-N-biosyl-beta-p-nitrophenyl, more genereal lacto-N-tetraose with 1-alcanols (methanol, ethanol, 1-propanol, 1-butanol) or p-nitrophenyl-beta-lacto-N-biose + lactose with enzyme
-
-
?
p-nitrophenyl-Gal-(1,3)-beta-GlcNAc + H2O
?
-
30% relative activity compared to p-nitrophenyl-lacto-N-bioside
-
-
?
p-nitrophenyl-lacto-N-bioside + H2O
p-nitrophenol + lacto-N-biose
-
most active substrate
-
-
?
p-nitrophenyl-lacto-N-bioside + H2O
p-nitrophenol + lacto-N-biose
-
-
-
?
p-nitrophenyl-lacto-N-bioside + H2O
p-nitrophenol + lacto-N-biose
-
-
-
-
?
p-nitrophenyl-lacto-N-bioside + H2O
p-nitrophenol + lacto-N-biose
-
-
-
?
p-nitrophenyl-lacto-N-bioside + H2O
p-nitrophenol + lacto-N-biose
-
-
-
-
?
pyridylamine-oligosaccharides which have type 1 chains at the nonreducing terminus + H2O
lacto-N-biose + ?
-
-
from N-acetyllactosamine type of triantennary sugar chain with type 1 structure and N-avcetyllactosamine type of biantennary sugar chain is produced
?
pyridylamine-oligosaccharides which have type 1 chains at the nonreducing terminus + H2O
lacto-N-biose + ?
-
no reaction with pyridylamine-oligosaccharides which contain only type 2 chains. No reaction with oligosaccharides in which the non-reducing terminal Gal or the penultimate GlcNAc are replaced by fucose or sialic acid are
-
-
?
pyridylamine-oligosaccharides which have type 1 chains at the nonreducing terminus + H2O
lacto-N-biose + ?
-
no reaction with pyridylamine-oligosaccharides which contain only type 2 chains. No reaction with oligosaccharides in which the non-reducing terminal Gal or the penultimate GlcNAc are replaced by fucose or sialic acid are
-
-
?
pyridylamine-oligosaccharides which have type 1 chains at the nonreducing terminus + H2O
lacto-N-biose + ?
-
-
from N-acetyllactosamine type of triantennary sugar chain with type 1 structure and N-avcetyllactosamine type of biantennary sugar chain is produced
?
sialyllacto-N-tetraose a + H2O
lactose + Fuc-alpha-(1->2)-Gal-beta-(1->3)[Fuc-alpha-(1->4)]GlcNAc
Neu5Ac-alpha-(2->3)-Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Gal
-
-
?
sialyllacto-N-tetraose a + H2O
lactose + Fuc-alpha-(1->2)-Gal-beta-(1->3)[Fuc-alpha-(1->4)]GlcNAc
Neu5Ac-alpha-(2->3)-Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Gal
-
-
?
additional information
?
-
-
human milk oligosaccharides are substrates and sole carbon source for Bifidobacterium bifidum colonizing the human intestinal tract. More than 130 types of human milk oligosaccharides have been isolated with the most abundant being lacto-N-tetraose, lacto-N-fucopentaose I, lacto-N-difucohexaose, and 2'-fucosyllactose
-
-
?
additional information
?
-
human milk oligosaccharides are substrates and sole carbon source for Bifidobacterium bifidum colonizing the human intestinal tract. More than 130 types of human milk oligosaccharides have been isolated with the most abundant being lacto-N-tetraose, lacto-N-fucopentaose I, lacto-N-difucohexaose, and 2'-fucosyllactose
-
-
?
additional information
?
-
-
human milk oligosaccharides are substrates and sole carbon source for Bifidobacterium bifidum colonizing the human intestinal tract. More than 130 types of human milk oligosaccharides have been isolated with the most abundant being lacto-N-tetraose, lacto-N-fucopentaose I, lacto-N-difucohexaose, and 2'-fucosyllactose
-
-
?
additional information
?
-
the enzyme releases a disaccharide
-
-
?
additional information
?
-
-
the enzyme releases a disaccharide
-
-
?
additional information
?
-
LnbB, a member of the glycoside hydrolase family 20 isolated from Bifidobacterium bifidum, releases Galbeta1-3GalNAc (GNB) from Gb5 and GA1 oligosaccharides. Substrate specificity, overview. Glycan-scavenging activity of LnbB, i.e. the activity of the enzyme towards the oligosaccharides of globo- and ganglio-series sphingolipids. Activity of GH20 LnbB towards Gb5 oligosaccharide is significantly low. No activity with Fuc-alpha-(1->2)-Gal-beta-(1->3)-GalNAc-beta-(1->3)-Gal-alpha-(1->4)-Gal-beta-(1->4)-Glc (Globo H) and Fuc-alpha-(1->2)Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc (LNFP I)
-
-
?
additional information
?
-
-
no activity on beta-linked p-nitrophenyl-monosaccharides, ganglioside GA1 structure with a beta-linked galacto-N-biose, fucosylated forms of lacto-N-tetraose or lacto-N-neoteraose
-
-
?
additional information
?
-
-
the recombinant enzyme shows substrate preference for the unmodified beta-linked lacto-biose I structure
-
-
?
additional information
?
-
the native substrate are human milk oligosaccharides. Among the different structures, four molecular species, namely 2'-fucosyllactose, lacto-N-tetraose, lacto-N-fucopentaose I, and lacto-N-difucohexaose I, are most abundantly present and comprise more than 50% of the total oligosaccharides, unless the milk is derived from non-secretor or Lewis-negative subjects
-
-
?
additional information
?
-
-
the native substrate are human milk oligosaccharides. Among the different structures, four molecular species, namely 2'-fucosyllactose, lacto-N-tetraose, lacto-N-fucopentaose I, and lacto-N-difucohexaose I, are most abundantly present and comprise more than 50% of the total oligosaccharides, unless the milk is derived from non-secretor or Lewis-negative subjects
-
-
?
additional information
?
-
the purified enzyme, which consists of LnbX only, hydrolyzes via a retaining mechanism the GlcNAcbeta-(1->3)-Gal linkage in lacto-N-tetraose, lacto-N-fucopentaose I, and sialyllacto-N-tetraose a. Inactive against lacto-N-neotetraose, lacto-N-triose II, lacto-N-fucopentaose II, and sialyllacto-N-tetraose b, substrate specificity, overview
-
-
?
additional information
?
-
-
the purified enzyme, which consists of LnbX only, hydrolyzes via a retaining mechanism the GlcNAcbeta-(1->3)-Gal linkage in lacto-N-tetraose, lacto-N-fucopentaose I, and sialyllacto-N-tetraose a. Inactive against lacto-N-neotetraose, lacto-N-triose II, lacto-N-fucopentaose II, and sialyllacto-N-tetraose b, substrate specificity, overview
-
-
?
additional information
?
-
the native substrate are human milk oligosaccharides. Among the different structures, four molecular species, namely 2'-fucosyllactose, lacto-N-tetraose, lacto-N-fucopentaose I, and lacto-N-difucohexaose I, are most abundantly present and comprise more than 50% of the total oligosaccharides, unless the milk is derived from non-secretor or Lewis-negative subjects
-
-
?
additional information
?
-
the purified enzyme, which consists of LnbX only, hydrolyzes via a retaining mechanism the GlcNAcbeta-(1->3)-Gal linkage in lacto-N-tetraose, lacto-N-fucopentaose I, and sialyllacto-N-tetraose a. Inactive against lacto-N-neotetraose, lacto-N-triose II, lacto-N-fucopentaose II, and sialyllacto-N-tetraose b, substrate specificity, overview
-
-
?
additional information
?
-
LnbX, a non-classified member of the glycoside hydrolase family, isolated from Bifidobacterium longum subsp. longum, liberates galacto-N-biose (GNB: Gal-beta-(1->3)-GalNAc) and 2'-fucosyl GNB (a type-4 trisaccharide) from Gb5 pentasaccharide and globo H hexasaccharide, respectively. Substrate specificity, overview. Glycan-scavenging activity of LnbX, i.e. the activity of the enzyme towards the oligosaccharides of globo- and ganglio-series sphingolipids. No activity with Gal-beta-(1->3)-GalNAc-beta-(1->4)-Gal-beta-(1->4)-Glc
-
-
?
additional information
?
-
-
no reaction with lacto-N-neotetraose, lacto-N-triose, sialyl lacto-N-tetraose, lacto-N-fucopentaose I, II, or III, asialo-GM1 tetrasaccharide, poly-N-acetyllactosamine
-
-
?
additional information
?
-
-
no reaction with lacto-N-neotetraose, lacto-N-triose, sialyl lacto-N-tetraose, lacto-N-fucopentaose I, II, or III, asialo-GM1 tetrasaccharide, poly-N-acetyllactosamine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-Gal-(1,3)-beta-GlcNAc-(1,3)-beta-D-Gal-(1,4)-D-Glc + H2O
lactose + D-galactosyl-beta-1,3-N-acetyl-D-glucosamine
lacto-N-fucopentaose I + H2O
lactose + Fuc-alpha-(1->2)-Gal-beta-(1->3)-GlcNAc
lacto-N-tetraose + H2O
lacto-N-biose + lactose
lacto-N-tetraose + H2O
lacto-N-biose I + lactose
-
-
-
?
lacto-N-tetraose + H2O
lactose + lacto-N-biose
sialyllacto-N-tetraose a + H2O
lactose + Fuc-alpha-(1->2)-Gal-beta-(1->3)[Fuc-alpha-(1->4)]GlcNAc
additional information
?
-
D-Gal-(1,3)-beta-GlcNAc-(1,3)-beta-D-Gal-(1,4)-D-Glc + H2O
lactose + D-galactosyl-beta-1,3-N-acetyl-D-glucosamine
lacto-N-tetraose, major component of human milk oligosaccharides
lacto-N-biose I
-
?
D-Gal-(1,3)-beta-GlcNAc-(1,3)-beta-D-Gal-(1,4)-D-Glc + H2O
lactose + D-galactosyl-beta-1,3-N-acetyl-D-glucosamine
-
lacto-N-tetraose, major component of human milk oligosaccharides
lacto-N-biose I
-
?
lacto-N-fucopentaose I + H2O
lactose + Fuc-alpha-(1->2)-Gal-beta-(1->3)-GlcNAc
Fuc-alpha-(1->2)-Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc
-
-
?
lacto-N-fucopentaose I + H2O
lactose + Fuc-alpha-(1->2)-Gal-beta-(1->3)-GlcNAc
Fuc-alpha-(1->2)-Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc
-
-
?
lacto-N-tetraose + H2O
lacto-N-biose + lactose
-
-
-
?
lacto-N-tetraose + H2O
lacto-N-biose + lactose
-
-
-
-
?
lacto-N-tetraose + H2O
lactose + lacto-N-biose
Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc
-
-
?
lacto-N-tetraose + H2O
lactose + lacto-N-biose
Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc
-
-
?
sialyllacto-N-tetraose a + H2O
lactose + Fuc-alpha-(1->2)-Gal-beta-(1->3)[Fuc-alpha-(1->4)]GlcNAc
Neu5Ac-alpha-(2->3)-Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Gal
-
-
?
sialyllacto-N-tetraose a + H2O
lactose + Fuc-alpha-(1->2)-Gal-beta-(1->3)[Fuc-alpha-(1->4)]GlcNAc
Neu5Ac-alpha-(2->3)-Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Gal
-
-
?
additional information
?
-
-
human milk oligosaccharides are substrates and sole carbon source for Bifidobacterium bifidum colonizing the human intestinal tract. More than 130 types of human milk oligosaccharides have been isolated with the most abundant being lacto-N-tetraose, lacto-N-fucopentaose I, lacto-N-difucohexaose, and 2'-fucosyllactose
-
-
?
additional information
?
-
human milk oligosaccharides are substrates and sole carbon source for Bifidobacterium bifidum colonizing the human intestinal tract. More than 130 types of human milk oligosaccharides have been isolated with the most abundant being lacto-N-tetraose, lacto-N-fucopentaose I, lacto-N-difucohexaose, and 2'-fucosyllactose
-
-
?
additional information
?
-
-
human milk oligosaccharides are substrates and sole carbon source for Bifidobacterium bifidum colonizing the human intestinal tract. More than 130 types of human milk oligosaccharides have been isolated with the most abundant being lacto-N-tetraose, lacto-N-fucopentaose I, lacto-N-difucohexaose, and 2'-fucosyllactose
-
-
?
additional information
?
-
the native substrate are human milk oligosaccharides. Among the different structures, four molecular species, namely 2'-fucosyllactose, lacto-N-tetraose, lacto-N-fucopentaose I, and lacto-N-difucohexaose I, are most abundantly present and comprise more than 50% of the total oligosaccharides, unless the milk is derived from non-secretor or Lewis-negative subjects
-
-
?
additional information
?
-
-
the native substrate are human milk oligosaccharides. Among the different structures, four molecular species, namely 2'-fucosyllactose, lacto-N-tetraose, lacto-N-fucopentaose I, and lacto-N-difucohexaose I, are most abundantly present and comprise more than 50% of the total oligosaccharides, unless the milk is derived from non-secretor or Lewis-negative subjects
-
-
?
additional information
?
-
the native substrate are human milk oligosaccharides. Among the different structures, four molecular species, namely 2'-fucosyllactose, lacto-N-tetraose, lacto-N-fucopentaose I, and lacto-N-difucohexaose I, are most abundantly present and comprise more than 50% of the total oligosaccharides, unless the milk is derived from non-secretor or Lewis-negative subjects
-
-
?
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.
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.
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.
evolution
the enzyme belongs to the glycoside hydrolase family 20, GH20
evolution
the LnbX protein is found only in Bifidobacterium bifidum, Bifidobacterium longum, and a few gut microbes, suggesting that the protein has evolved in specialized niches
evolution
LnbB is a member of the glycoside hydrolase family 20, GH20
evolution
LnbX is a non-classified member of the glycoside hydrolase family
evolution
the enzyme belongs to the glycosyl hydrolase family 20, GH20
evolution
the enzyme belongs to the glycosyl hydrolase family 20, GH20. Domain organization of GH20 beta-N-acetylhexosaminidases, overview
evolution
-
the LnbX protein is found only in Bifidobacterium bifidum, Bifidobacterium longum, and a few gut microbes, suggesting that the protein has evolved in specialized niches
-
metabolism
-
the enzyme is critical in the lacto-N-biose pathway
metabolism
the enzyme liberates lacto-N-biose I, i.e. Gal-beta-(1->3)-GlcNAc, the major core structure, from the nonreducing end of human milk oligosaccharides and plays a key role in the metabolic pathway of these compounds
physiological function
the enzyme liberates lacto-N-biose I, the major core structure, from the nonreducing end of human milk oligosaccharides and plays a key role in the metabolic pathway of these compounds
physiological function
lacto-N-biosidase (LNBase), a beta-N-acetyl-hexosaminidase that liberates lacto-N-biose (LNB) from human milk oligosaccharides (HMOs), is important to the LNB pathway
physiological function
lacto-N-biosidase is a key enzyme that degrades lacto-N-tetraose, a main component of human milk oligosaccharides (HMOs, the third-most abundant solid component in human milk), into lacto-N-biose I and lactose. . Enzymatic release of beta-linked GNB from natural substrates, these unique activities may play a role in modulating the microbial composition in the gut ecosystem
physiological function
lacto-N-biosidase is a key enzyme that degrades lacto-N-tetraose, a main component of human milk oligosaccharides (HMOs, the third-most abundant solid component in human milk), into lacto-N-biose I and lactose. Enzymatic release of beta-linked Galbeta1-3GalNAc from natural substrates, these unique activities may play a role in modulating the microbial composition in the gut ecosystem
additional information
the enzyme reaction proceeds via a substrate-assisted catalytic mechanism. The enzyme consists of three domains, and the C-terminal domain has a unique beta-trefoil-like fold. Compared with other beta-N-acetylhexosaminidases, lacto-N-biosidase has a wide substrate-binding pocket with a -2 subsite specific for beta-1,3-linked Gal, three-dimensional structure and possible conformational pathway for the lacto-N-biosidase reaction, overview. Enzyme structure and active site structure comparisons. The two catalytic residues of GH20, Asp320 (polarizing residue) and Glu321 (acid/base catalytic residue), form hydrogen bonds with the amide nitrogen of the 2-acetamido group and the O1-hydroxyl,respectively. Tyr-419 is a highly conserved residue in GH20 enzymes, and its side-chain hydroxyl group forms a hydrogen bond with the carbonyl oxygen atom of the 2-acetamido group. Asp467 forms bifurcated hydrogen bonds with the O4- and O6-hydroxyl groups of the GlcNAc residue. Catalytic reaction mechanism and conformational changes analysis
additional information
-
the enzyme reaction proceeds via a substrate-assisted catalytic mechanism. The enzyme consists of three domains, and the C-terminal domain has a unique beta-trefoil-like fold. Compared with other beta-N-acetylhexosaminidases, lacto-N-biosidase has a wide substrate-binding pocket with a -2 subsite specific for beta-1,3-linked Gal, three-dimensional structure and possible conformational pathway for the lacto-N-biosidase reaction, overview. Enzyme structure and active site structure comparisons. The two catalytic residues of GH20, Asp320 (polarizing residue) and Glu321 (acid/base catalytic residue), form hydrogen bonds with the amide nitrogen of the 2-acetamido group and the O1-hydroxyl,respectively. Tyr-419 is a highly conserved residue in GH20 enzymes, and its side-chain hydroxyl group forms a hydrogen bond with the carbonyl oxygen atom of the 2-acetamido group. Asp467 forms bifurcated hydrogen bonds with the O4- and O6-hydroxyl groups of the GlcNAc residue. Catalytic reaction mechanism and conformational changes analysis
additional information
-
three realistic mechanistic alternatives exist for lacto-N-biosidases: substrate-assisted catalytic mechanism, or a mechanism involving the formation and breakdown of a covalent aglycosyl enzyme intermediate, or an inverting mechanism, overview. A key difference between these mechanistic alternatives is the involvement of the 2-acetamido group of the substrate. The lacto-N-biosidase-type enzyme uses a mechanism involving substrate-assisted catalysis from the 2-acetamido group of the substrate. Decrease in second-order rate constant, the carbonyl oxygen acts as a nucleophile, attacking the anomeric centre
additional information
the large Bifidobacterium bifidum lacto-N-biosidase and its truncated mutants are used as model proteins to evaluate the minimal functional unit due to its interest and structural complexity. Structure-function analysis of the wild-type in comparison to different truncated enzyme mutants, and comparisons of enzyme structure models, overview. The lacto-N-biosidase requires GH20b and the lectin-like domain at the N- and C-termini of the catalytic GH20 domain to be fully soluble and functional. The lectin domain provides this remote element to the active site. Restoration of activity of the inactive GH20beta-GH20-alpha construct (model A architecture) by a complementation assay with the lectin-like domain
additional information
-
the large Bifidobacterium bifidum lacto-N-biosidase and its truncated mutants are used as model proteins to evaluate the minimal functional unit due to its interest and structural complexity. Structure-function analysis of the wild-type in comparison to different truncated enzyme mutants, and comparisons of enzyme structure models, overview. The lacto-N-biosidase requires GH20b and the lectin-like domain at the N- and C-termini of the catalytic GH20 domain to be fully soluble and functional. The lectin domain provides this remote element to the active site. Restoration of activity of the inactive GH20beta-GH20-alpha construct (model A architecture) by a complementation assay with the lectin-like domain
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.
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.
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.
Sano, M.; Hayakawa, K.; Kato, I.
Purification and characterization of an enzyme releasing lacto-N-biose from oligosaccharides with type 1 chain
J. Biol. Chem.
268
18560-18566
1993
Streptomyces sp., Streptomyces sp. 142
brenda
Sano, M.; Hayakawa, K.; Kato, I.
An enzyme releasing lacto-N-biose from oligosaccharides
Proc. Natl. Acad. Sci. USA
89
8512-8516
1992
Streptomyces sp., Streptomyces sp. 142
brenda
Murata, T.; Inukai, T.; Suzuki, M.; Yamagishi, M.; Usui, A.T.
Facile enzymatic conversion of lactose into lacto-N-tetraose and lacto-N-neotetraose
Glycoconj. J.
16
189-195
1999
Microbacterium sp., Microbacterium sp. L-101
brenda
Wada, J.; Ando, T.; Kiyohara, M.; Ashida, H.; Kitaoka, M.; Yamaguchi, M.; Kumagai, H.; Katayama, T.; Yamamoto, K.
Bifidobacterium bifidum lacto-N-biosidase, a critical enzyme for the degradation of human milk oligosaccharides with a type 1 structure
Appl. Environ. Microbiol.
74
3996-4004
2008
Bifidobacterium longum, Bifidobacterium bifidum JCM 1254, no activity in Bifidobacterium breve, no activity in Bifidobacterium catenulatum, Bifidobacterium bifidum (B3TLD6), Bifidobacterium bifidum
brenda
Hattie, M.; Debowski, A.W.; Stubbs, K.A.
Development of tools to study lacto-N-biosidase: an important enzyme involved in the breakdown of human milk oligosaccharides
ChemBioChem
13
1128-1131
2012
Bifidobacterium bifidum
brenda
Ito, T.; Katayama, T.; Hattie, M.; Sakurama, H.; Wada, J.; Suzuki, R.; Ashida, H.; Wakagi, T.; Yamamoto, K.; Stubbs, K.A.; Fushinobu, S.
Crystal structures of a glycoside hydrolase family 20 lacto-N-biosidase from Bifidobacterium bifidum
J. Biol. Chem.
288
11795-11806
2013
Bifidobacterium bifidum (B3TLD6), Bifidobacterium bifidum
brenda
Sakurama, H.; Kiyohara, M.; Wada, J.; Honda, Y.; Yamaguchi, M.; Fukiya, S.; Yokota, A.; Ashida, H.; Kumagai, H.; Kitaoka, M.; Yamamoto, K.; Katayama, T.
Lacto-N-biosidase encoded by a novel gene of Bifidobacterium longum subspecies longum shows unique substrate specificity and requires a designated chaperone for its active expression
J. Biol. Chem.
288
25194-25206
2013
Bifidobacterium longum (A0A024QYS6), Bifidobacterium longum, Bifidobacterium longum JCM 1217 (A0A024QYS6)
brenda
Gotoh, A.; Katoh, T.; Sugiyama, Y.; Kurihara, S.; Honda, Y.; Sakurama, H.; Kambe, T.; Ashida, H.; Kitaoka, M.; Yamamoto, K.; Katayama, T.
Novel substrate specificities of two lacto-N-biosidases towards beta-linked galacto-N-biose-containing oligosaccharides of globo H, Gb5, and GA1
Carbohydr. Res.
408
18-24
2015
Bifidobacterium longum subsp. Longum (A0A024QYS6), Bifidobacterium bifidum (B3TLD6)
brenda
Hattie, M.; Ito, T.; Debowski, A.W.; Arakawa, T.; Katayama, T.; Yamamoto, K.; Fushinobu, S.; Stubbs, K.A.
Gaining insight into the catalysis by GH20 lacto-N-biosidase using small molecule inhibitors and structural analysis
Chem. Commun. (Camb.)
51
15008-15011
2015
Bifidobacterium bifidum (B3TLD6)
brenda
Val-Cid, C.; Biarnes, X.; Faijes, M.; Planas, A.
Structural-functional analysis reveals a specific domain organization in family GH20 hexosaminidases
PLoS ONE
10
e0128075
2015
Bifidobacterium bifidum (B3TLD6), Bifidobacterium bifidum
brenda