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Information on EC 2.4.1.211 - 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase
for references in articles please use BRENDA:EC2.4.1.211
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.211 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase
IUBMB Comments
Reaction also occurs with β-D-galactopyranosyl-(1→3)-N-acetyl-D-galactosamine as the substrate, giving N-acetyl-D-galactosamine as the product.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 2.4.1.211
-
glutamine-binding
- longum
-
ligand-free
- l-glutamine
-
4-epimerase
- synthesis
-
uridylyltransferase
- galnac
-
bifidobacterial
-
ligand-bound
- bifidus
- phosphorylases
- biotechnology
- nutrition
- medicine
Reaction Schemes
showSynonyms
glnbp, lacto-n-biose phosphorylase, gl-bp, galacto-n-biose/lacto-n-biose i phosphorylase, galacto-n-biose phosphorylase, gnb/lnb phosphorylase, beta-1,3-galactosyl-n-acetylhexosamine phosphorylase, galhexnacp, lacto-n-biose i phosphorylase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,3-beta-galactosyl-N-acetylhexosamine phosphorylase
beta-1,3-galactosyl-N-acetylhexosamine phosphorylase
beta-D-galactopyranosyl-(1-3)-N-acetyl-D-hexosamine:phosphate galactosyltransferase
-
-
-
-
BLLJ-1623
D-galactosyl-beta1,3-N-acetyl-D-hexosamine phosphorylase
-
Gal-GlyNAcP
galacto-N-biose phosphorylase
galacto-N-biose/lacto-N-biose I phosphorylase
galacto-N-biose/LNB phosphorylase
GalHexNAcP
GL-BP
GLNBP
GNB/LNB phosphorylase
GnpA
lacto-N-biose I phosphorylase
lacto-N-biose phosphorylase
lnba
LNBP
N-biose/lacto-N-biose I-binding protein
1,3-beta-galactosyl-N-acetylhexosamine phosphorylase
-
-
1,3-beta-galactosyl-N-acetylhexosamine phosphorylase
-
-
-
galacto-N-biose/lacto-N-biose I phosphorylase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-D-galactopyranosyl-(1->3)-N-acetyl-D-glucosamine + phosphate = alpha-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine
beta-D-galactopyranosyl-(1->3)-N-acetyl-D-glucosamine + phosphate = alpha-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine
reaction also occurs with beta-D-galactopyranosyl-(1->3)-N-acetyl-D-galactosamine as the substrate, giving N-acetyl-D-galactosamine as the product
-
beta-D-galactopyranosyl-(1->3)-N-acetyl-D-glucosamine + phosphate = alpha-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
beta-D-galactopyranosyl-(1->3)-N-acetyl-D-hexosamine:phosphate galactosyltransferase
Reaction also occurs with beta-D-galactopyranosyl-(1->3)-N-acetyl-D-galactosamine as the substrate, giving N-acetyl-D-galactosamine as the product.
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CAS REGISTRY NUMBER
COMMENTARY
224427-06-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine
beta-D-galactopyranosyl-(1->3)-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
lacto-N-biose + phosphate
-
Substrates: -
Products: -
Products: -
?
alpha-D-galactose 1-phosphate + N-acetyl-galactosamine
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine + phosphate
beta D-galactosido-(1,3)-N-acetylgalactosamine + H2O
alpha-D-galactose-1-phosphate + GalNAc
-
Substrates: -
Products: -
Products: -
r
beta-D-galactopyranosyl-(1->3)-N-acetyl-D-glucosamine + phosphate
alpha-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine + phosphate
alpha-D-galactopyranose 1-phosphate + N-acetyl-D-galactosamine
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-galactosamine
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-galactosamine
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-galactosamine
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-glucosamine
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosoamine + phosphate
alpha-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine
alpha-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine
beta-D-galactopyranosyl-(1->3)-N-acetyl-D-glucosamine + phosphate
Substrates: -
Products: -
Products: -
?
alpha-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine
beta-D-galactopyranosyl-(1->3)-N-acetyl-D-glucosamine + phosphate
Substrates: -
Products: -
Products: -
?
alpha-D-galactose 1-phosphate + N-acetyl-galactosamine
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine + phosphate
-
Substrates: -
Products: -
Products: -
?
alpha-D-galactose 1-phosphate + N-acetyl-galactosamine
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine + phosphate
-
Substrates: -
Products: -
Products: -
?
alpha-D-galactose 1-phosphate + N-acetyl-galactosamine
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine + phosphate
Substrates: -
Products: -
Products: -
r
alpha-D-galactose 1-phosphate + N-acetyl-galactosamine
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine + phosphate
Substrates: -
Products: -
Products: -
r
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine + phosphate
alpha-D-galactopyranose 1-phosphate + N-acetyl-D-galactosamine
Substrates: -
Products: -
Products: -
r
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine + phosphate
alpha-D-galactopyranose 1-phosphate + N-acetyl-D-galactosamine
Substrates: -
Products: -
Products: -
r
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-galactosamine
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-galactosamine
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-galactosamine
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-galactosamine
Substrates: GnpA shows approximately 70times higher specific activity of phosphorolysis on beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine than that on beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine
Products: specific activity on N-acetyl-D-galactosamine is approximately 60times higher than that on N-acetyl-D-glucosamine
Products: specific activity on N-acetyl-D-galactosamine is approximately 60times higher than that on N-acetyl-D-glucosamine
r
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-galactosamine
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-galactosamine
Substrates: GnpA shows approximately 70times higher specific activity of phosphorolysis on beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine than that on beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine
Products: specific activity on N-acetyl-D-galactosamine is approximately 60times higher than that on N-acetyl-D-glucosamine
Products: specific activity on N-acetyl-D-galactosamine is approximately 60times higher than that on N-acetyl-D-glucosamine
r
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-galactosamine
Cutibacterium acnes JCM 6473
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-galactosamine
Substrates: beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine is galacto-N-biose
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-galactosamine
Substrates: beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine is galacto-N-biose
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-galactosamine
-
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-galactosamine
-
Substrates: the gene operon for LNBP lnpABCD encodes a lacto-N-biose I and beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine metabolic pathway with lacto-N-biose phosphorylase, N-acetylhexosamine 1-kinase, UDP-glucose hexose 1-phosphate uridylyltransferase, and UDP-glucose 4-epimerase, this pathway is involved in the intestinal colonization of bifidobacteria and utilizes lacto-N-biose I from human milk oligosaccharides or beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine from mucin sugars
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-galactosamine
-
Substrates: the gene operon for LNBP lnpABCD encodes a lacto-N-biose I and beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine metabolic pathway with lacto-N-biose phosphorylase, N-acetylhexosamine 1-kinase, UDP-glucose hexose 1-phosphate uridylyltransferase, and UDP-glucose 4-epimerase, this pathway is involved in the intestinal colonization of bifidobacteria and utilizes lacto-N-biose I from human milk oligosaccharides or beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine from mucin sugars
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-galactosamine
-
Substrates: no activity with D-glucose, D-glucosamine, D-fructose, 2-deoxy-D-glucose, D-mannose, maltose, and sucrose as substrates
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-galactosamine
-
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-galactosamine
Substrates: -
Products: -
Products: -
r
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-galactosamine
Substrates: -
Products: -
Products: -
r
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-galactosamine
-
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
Substrates: GnpA shows approximately 70times higher specific activity of phosphorolysis on beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine than that on beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine
Products: -
Products: -
r
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
Substrates: GnpA shows approximately 70times higher specific activity of phosphorolysis on beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine than that on beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine
Products: -
Products: -
r
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
Cutibacterium acnes JCM 6473
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
Substrates: beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine is lacto-N-biose I, best substrate being 7times more effective than beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
Substrates: beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine is lacto-N-biose I, best substrate being 7times more effective than beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-glucosamine
-
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-glucosamine
-
Substrates: -
Products: -
Products: -
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosoamine + phosphate
alpha-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine
-
Substrates: hydrolysis involves a Walden inversion
Products: -
Products: -
r
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosoamine + phosphate
alpha-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine
Substrates: -
Products: -
Products: -
r
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosoamine + phosphate
alpha-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine
Substrates: -
Products: -
Products: -
r
galacto-N-biose + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-galactosamine
Substrates: -
Products: -
Products: -
?
galacto-N-biose + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-galactosamine
Substrates: -
Products: -
Products: -
r
lacto-N-biose I + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
Substrates: -
Products: -
Products: -
?
lacto-N-biose I + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
Substrates: -
Products: -
Products: -
r
lacto-N-biose I + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity, overview. Structurally determined substrate preference for galacto-N-biose and lacto-N-biose I
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme reversibly phosphorolyzes galacto-N-biose (Galbeta1, 3GalNAc, GNB) and/or lacto-N-biose I (Galbeta1,3GlcNAc,LNB) to form alpha-galactose 1-phosphate (Gal1P) and the corresponding N-acetylhexosamine
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme reversibly phosphorolyzes galacto-N-biose (Galbeta1, 3GalNAc, GNB) and/or lacto-N-biose I (Galbeta1,3GlcNAc,LNB) to form alpha-galactose 1-phosphate (Gal1P) and the corresponding N-acetylhexosamine
Products: -
Products: -
?
additional information
?
-
Substrates: GnpA shows a weak activity on alpha-N-acetylgalactosaminyl-O-serine and does not exhibit significant activity (kcat less than 0.1 s-1) on D-galactose, D-glucose, glucosamine, 2-deoxy-glucose, D-fructose, mannose, maltose, and sucrose, N-acetylgalactosamine 6-sulfate, and N-acetylglucosamine 6-sulfate, GnpA does not act on either D-glucose 1-phosphate or N-acetyl-D-glucosamine 1-phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: GnpA shows a weak activity on alpha-N-acetylgalactosaminyl-O-serine and does not exhibit significant activity (kcat less than 0.1 s-1) on D-galactose, D-glucose, glucosamine, 2-deoxy-glucose, D-fructose, mannose, maltose, and sucrose, N-acetylgalactosamine 6-sulfate, and N-acetylglucosamine 6-sulfate, GnpA does not act on either D-glucose 1-phosphate or N-acetyl-D-glucosamine 1-phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: GnpA shows a weak activity on alpha-N-acetylgalactosaminyl-O-serine and does not exhibit significant activity (kcat less than 0.1 s-1) on D-galactose, D-glucose, glucosamine, 2-deoxy-glucose, D-fructose, mannose, maltose, and sucrose, N-acetylgalactosamine 6-sulfate, and N-acetylglucosamine 6-sulfate, GnpA does not act on either D-glucose 1-phosphate or N-acetyl-D-glucosamine 1-phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: GnpA shows a weak activity on alpha-N-acetylgalactosaminyl-O-serine and does not exhibit significant activity (kcat less than 0.1 s-1) on D-galactose, D-glucose, glucosamine, 2-deoxy-glucose, D-fructose, mannose, maltose, and sucrose, N-acetylgalactosamine 6-sulfate, and N-acetylglucosamine 6-sulfate, GnpA does not act on either D-glucose 1-phosphate or N-acetyl-D-glucosamine 1-phosphate
Products: -
Products: -
?
additional information
?
-
Cutibacterium acnes JCM 6473
Substrates: GnpA shows a weak activity on alpha-N-acetylgalactosaminyl-O-serine and does not exhibit significant activity (kcat less than 0.1 s-1) on D-galactose, D-glucose, glucosamine, 2-deoxy-glucose, D-fructose, mannose, maltose, and sucrose, N-acetylgalactosamine 6-sulfate, and N-acetylglucosamine 6-sulfate, GnpA does not act on either D-glucose 1-phosphate or N-acetyl-D-glucosamine 1-phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: Cphy0577 protein does not show activity on either L-Rha, D-Glc, or D-Gal
Products: -
Products: -
?
additional information
?
-
Substrates: Cphy0577 protein does not show activity on either L-Rha, D-Glc, or D-Gal
Products: -
Products: -
?
additional information
?
-
-
Substrates: Cphy0577 protein does not show activity on either L-Rha, D-Glc, or D-Gal
Products: -
Products: -
?
additional information
?
-
Substrates: Cphy3030 protein does not show activity on either L-Rha, D-Glc, or D-Gal
Products: -
Products: -
?
additional information
?
-
Substrates: Cphy3030 protein does not show activity on either L-Rha, D-Glc, or D-Gal
Products: -
Products: -
?
additional information
?
-
-
Substrates: Cphy3030 protein does not show activity on either L-Rha, D-Glc, or D-Gal
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with D-glucose, D-galactose, D-glucosamine, D-fructose, 2-deoxy-D-glucose, D-mannose, maltose, and sucrose
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with D-glucose, D-galactose, D-glucosamine, D-fructose, 2-deoxy-D-glucose, D-mannose, maltose, and sucrose
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Substrates: the enzyme reversibly phosphorolyzes galacto-N-biose (Galbeta1, 3GalNAc, GNB) and/or lacto-N-biose I (Galbeta1,3GlcNAc,LNB) to form alpha-galactose 1-phosphate (Gal1P) and the corresponding N-acetylhexosamine
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme reversibly phosphorolyzes galacto-N-biose (Galbeta1, 3GalNAc, GNB) and/or lacto-N-biose I (Galbeta1,3GlcNAc,LNB) to form alpha-galactose 1-phosphate (Gal1P) and the corresponding N-acetylhexosamine
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.72
alpha-D-galactose 1-phosphate
wild type enzyme, using N-acetyl-D-glucosamine as cosubstrate
17
alpha-D-galactose 1-phosphate
mutant enzyme Y362F, using N-acetyl-D-glucosamine as cosubstrate
19
alpha-D-galactose 1-phosphate
mutant enzyme F364N, using N-acetyl-D-glucosamine as cosubstrate
24
alpha-D-galactose 1-phosphate
mutant enzyme N166A, using N-acetyl-D-glucosamine as cosubstrate
10
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine
in 50 mM Tris-HCl (pH 7.5), 10 mM sodium-potassium phosphate buffer, at 30°C
140
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine
in 100 mM MOPS buffer (pH 7.0) at 37°C
1.7
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine
-
sequential bi-bi mechanism
5.6
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine
-
-
2.1
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine
-
-
3.6
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine
in 50 mM Tris-HCl (pH 7.5), 10 mM sodium-potassium phosphate buffer, at 30°C
1300
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine
in 100 mM MOPS buffer (pH 7.0) at 37°C
11
N-acetyl-D-galactosamine
in 100 mM MOPS buffer (pH 7.0) at 37°C
130
N-acetyl-D-glucosamine
in 100 mM MOPS buffer (pH 7.0) at 37°C
0.064
phosphate
with beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine as cosubstrate, in 50 mM Tris-HCl (pH 7.5), 10 mM sodium-potassium phosphate buffer, at 30°C
0.43
phosphate
-
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine as substrate
0.52
phosphate
-
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine as substrate
0.58
phosphate
-
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine as substrate
0.66
phosphate
-
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine as substrate
1.3
phosphate
with beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine as cosubstrate, in 50 mM Tris-HCl (pH 7.5), 10 mM sodium-potassium phosphate buffer, at 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.09
alpha-D-galactose 1-phosphate
mutant enzyme Y362F, using N-acetyl-D-glucosamine as cosubstrate
0.3
alpha-D-galactose 1-phosphate
mutant enzyme N166A, using N-acetyl-D-glucosamine as cosubstrate
4.83
alpha-D-galactose 1-phosphate
mutant enzyme F364N, using N-acetyl-D-glucosamine as cosubstrate
10.7
alpha-D-galactose 1-phosphate
wild type enzyme, using N-acetyl-D-glucosamine as cosubstrate
2.2
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine
in 50 mM Tris-HCl (pH 7.5), 10 mM sodium-potassium phosphate buffer, at 30°C
103
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine
in 100 mM MOPS buffer (pH 7.0) at 37°C
14
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine
in 100 mM MOPS buffer (pH 7.0) at 37°C
45
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine
in 50 mM Tris-HCl (pH 7.5), 10 mM sodium-potassium phosphate buffer, at 30°C
42
N-acetyl-D-galactosamine
in 100 mM MOPS buffer (pH 7.0) at 37°C
5.9
N-acetyl-D-glucosamine
in 100 mM MOPS buffer (pH 7.0) at 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.9
N-acetyl-D-galactosamine
in 100 mM MOPS buffer (pH 7.0) at 37°C
0.044
N-acetyl-D-glucosamine
in 100 mM MOPS buffer (pH 7.0) at 37°C
0.005
alpha-D-galactose 1-phosphate
mutant enzyme Y362F, using N-acetyl-D-glucosamine as cosubstrate
0.012
alpha-D-galactose 1-phosphate
mutant enzyme N166A, using N-acetyl-D-glucosamine as cosubstrate
0.26
alpha-D-galactose 1-phosphate
mutant enzyme F364N, using N-acetyl-D-glucosamine as cosubstrate
6.21
alpha-D-galactose 1-phosphate
wild type enzyme, using N-acetyl-D-glucosamine as cosubstrate
0.22
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine
in 50 mM Tris-HCl (pH 7.5), 10 mM sodium-potassium phosphate buffer, at 30°C
0.73
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine
in 100 mM MOPS buffer (pH 7.0) at 37°C
0.01
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine
in 100 mM MOPS buffer (pH 7.0) at 37°C
13
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine
in 50 mM Tris-HCl (pH 7.5), 10 mM sodium-potassium phosphate buffer, at 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0002
-
D313N, no activity, D313 is probably the catalytic proton donor site
10
10.5
-
LNBP1, all mutants display decreased activities, D313N has no activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 60
temperature-activity profiles of recombinant wild-type and mutant enzymes, overview
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subspecies Bifidobacterium longum longum and subspecies Bifidobacterium longum infantis
-
-
brenda
gene lnpA, located in a gene cluster encoding a specific pathway for utilization of galacto-N-biose and lacto-N-biose
UniProt
brenda
gene lnpA, located in a gene cluster encoding a specific pathway for utilization of galacto-N-biose and lacto-N-biose
UniProt
brenda
bacterium possesses three GalHexNAcP homologous genes, cphy0577 gene; anaerobic cellulolytic bacterium
UniProt
brenda
bacterium possesses three GalHexNAcP homologous genes, Cphy3030 gene; anaerobic cellulolytic bacterium
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
proteins are predicted not to possess N-terminal signal peptides
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the GalHexNAcP belongs to the glycoside hydrolase family 112, GH112
metabolism
physiological function
additional information
the residues at positions 162, 161, and 336 determine the substrate specificity, structure-function relationship, molecular docking, and specificity prediction, overview. The side-chain hydroxyl group of S336 forms a hydrogen bond with the side-chain nitrogen atom of R358, which plays a significant role in catalysis
metabolism
the enzyme is important in the specific pathway for utilization of galacto-N-biose and lacto-N-biose, the latter is a major structural disaccharide in the core structures of human milk oligosaccharides
metabolism
-
the enzyme is important in the specific pathway for utilization of galacto-N-biose and lacto-N-biose, the latter is a major structural disaccharide in the core structures of human milk oligosaccharides
-
physiological function
key enzyme for intestinal growth, phosphorolyses galacto-N-biose and lacto-N-biose I with anomeric inversion
physiological function
-
GLNBP plays a key role in the colonization of bifidobacteria in the infant intestine
physiological function
-
GLNBP plays a key role in the colonization of bifidobacteria in the infant intestine
physiological function
-
GLNBP plays a key role in the colonization of bifidobacteria in the infant intestine
physiological function
key enzyme in the enzymatic production of lacto-N-biose I
physiological function
-
key enzyme in the enzymatic production of lacto-N-biose I
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GAHP2_LACP7
Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
723
0
83896
Swiss-Prot
Secretory Pathway (Reliability: 1)
GAHP1_LACP7
Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
724
0
83856
Swiss-Prot
-
LNPA_BIFL2
Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b)
751
0
84327
Swiss-Prot
Secretory Pathway (Reliability: 5)
A0A3Q0KZS1_VIBVU
Vibrio vulnificus (strain CMCP6)
728
0
83583
TrEMBL
-
B7XEJ0_CUTAC
738
0
82127
TrEMBL
Secretory Pathway (Reliability: 3)
B7XEJ1_CUTAC
738
0
82140
TrEMBL
other Location (Reliability: 3)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000
83480
His-tagged enzyme, calculated from amino acid sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine and beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine
sitting drop vapor diffusion method, using 0.1 M sodium cacodylate (pH 6.5), 0.2 M Mg(NO3)2, and 15% (v/v) polyethylene glycol 4000
purified recombinant enzyme mutant C236Y, X-ray diffraction structure determination and analysis at 2.6 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P161S
site-directed mutagenesis, the mutation leads to an increase in the selectivity on lacto-N-biose I
S336A
site-directed mutagenesis, the mutation leads to an increase in the selectivity on lacto-N-biose I
V162T
site-directed mutagenesis, the mutation leads to an increase in the selectivity on galacto-N-biose
Y362F
the mutation results in about 1000fold reduction of the catalytic efficiency
Y362N
the mutation results in the complete loss of the activity
C236E
random mutagenesis, the mutant shows decreased thermostability and reduced activity compared to the wild-type
C236F
random mutagenesis, the mutant shows highly increased thermostability and inacreased activity compared to the wild-type
C236H
random mutagenesis, the mutant shows slightly increased thermostability compared to the wild-type
C236P
random mutagenesis, the mutant shows highly increased thermostability and reduced activity compared to the wild-type
C236W
random mutagenesis, the mutant shows slightly increased thermostability compared to the wild-type
C236Y
random mutagenesis, the mutant shows highly increased thermostability and increased activity compared to the wild-type. In the mutant, the hydroxyl group of Tyr236 forms a hydrogen bond with the carboxyl group of E319. Mutant C236Y shows a 1.6fold higher specific activity than the wild-type
C236Y/D576V
random mutagenesis, the mutant shows highly increased thermostability compared to the wild-type
D576A
random mutagenesis, the mutant shows highly increased thermostability compared to the wild-type
D576F
random mutagenesis, the mutant shows highly increased thermostability and reduced activity compared to the wild-type
D576G
random mutagenesis, the mutant shows highly increased thermostability and increased activity compared to the wild-type
D576I
random mutagenesis, the mutant shows highly increased thermostability compared to the wild-type
D576L
random mutagenesis, the mutant shows highly increased thermostability compared to the wild-type
D576M
random mutagenesis, the mutant shows highly increased thermostability compared to the wild-type
D576P
random mutagenesis, the mutant shows decreased thermostability compared to the wild-type
D576V
random mutagenesis, the mutant shows highly increased thermostability compared to the wild-type
D576W
random mutagenesis, the mutant shows highly increased thermostability and reduced activity compared to the wild-type
G437S
random mutagenesis, the mutant shows slightly increased thermostability and slightly reducd activity compared to the wild-type
N506S
random mutagenesis, the mutant shows slightly increased thermostability and reduced activity compared to the wild-type
R290H
random mutagenesis, the mutant shows slightly increased thermostability and slightly reduced activity compared to the wild-type
R290H/G437S/N506S
random mutagenesis, the mutant shows highly increased thermostability and reduced activity compared to the wild-type
C236Y
-
random mutagenesis, the mutant shows highly increased thermostability and increased activity compared to the wild-type. In the mutant, the hydroxyl group of Tyr236 forms a hydrogen bond with the carboxyl group of E319. Mutant C236Y shows a 1.6fold higher specific activity than the wild-type
-
C236Y/D576V
-
random mutagenesis, the mutant shows highly increased thermostability compared to the wild-type
-
D576V
-
random mutagenesis, the mutant shows highly increased thermostability compared to the wild-type
-
R290H
-
random mutagenesis, the mutant shows slightly increased thermostability and slightly reduced activity compared to the wild-type
-
additional information
additional information
enzyme engineering for improved thermostability, random mutagenesis GLNBP library construction using error-prone polymerase chain reaction and mutant screening, overview
additional information
-
enzyme engineering for improved thermostability, random mutagenesis GLNBP library construction using error-prone polymerase chain reaction and mutant screening, overview
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7.5
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 55
the enzyme is stable at temperatures up to 30°C during incubation for 30 min, the reactions proceed linearly for 5 min at temperatures up to 37°C but do not proceed linearly at 45°C, no reaction is observed at 55°C
55
rapid inactivation of wild-type enzyme, slower inactivation of mutants R209H, G437S, and N506S, mutants C236Y and D576V retain some activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
of the recombinant protein by Ni-nitrilotriacetic acid agarose column chromatography
-
of the recombinant protein by Ni-NTA spin column chromatography
-
of the recombinant proteins by Ni-NTA spin column chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, exxpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
expression in Escherichia coli
gene lnpA, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain strain BL21
the non-labeled enzyme is expressed in Escherichia coli BL21(DE3) cells, the selenomethionine-labeled enzyme is expressed in Escherichia coli strain B834 (DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
LNBP is cultured with sucrose phosphorylase, UDP-glucose hexose 1-phosphate uridylyltransferase, and UDP-glucose 4-epimerase to produce beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine using sucrose as substrate in a 10l reaction mixture, 500 mmol beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine are produced after 600 h, beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine can be used as bifidus factor in human milk
medicine
-
galactosyl-N-acetylhexosamine phosphorylase has a predominant role in the digestive tract of human and in the metabolism of galactose
nutrition
-
dairy industry production of different fermented bifidobacteria milks
synthesis
synthesis
-
production of dissaccharidic structures instead of chemical synthesis
synthesis
suitable catalyst for practical syntheses of oligosaccharides
synthesis
large scale production of lacto-N-biose I, a building block of type I human milk oligosaccharides
synthesis
-
production of lactobiose I by mixing crude extracts containing 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase, sucrose phosphorylase, UDP-glucose-hexose 1-phosphate uridylyltransferase, and UDP-glucose 4-epimerase, each recombinantly produced by Escherichia coli. The first two interfering enzymes are selectively inactivated by heat treatment at 47°C for 1 h in the presence of pancreatin, and glycogen phosphorylase is disabled by hydrolyzing its possible acceptor molecules using glucoamylase. 91 % of GlcNAc are converted in the 100-ml reaction mixture containing 300 mM GlcNAc
synthesis
-
large scale production of lacto-N-biose I, a building block of type I human milk oligosaccharides
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Derensy-Dron, D.; Krzewinski, F.; Brassart, C.; Bouquelet, S.
beta-1,3-Galactosyl-N-acetylhexosamine phosphorylase from Bifidobacterium bifidum DSM 20082: characterization, partial purification and relation to mucin degradation
Biotechnol. Appl. Biochem.
29
3-10
1999
Bifidobacterium bifidum
brenda
Kitaoka, M.; Tian, J.; Nishimoto, M.
Novel putative galactose operon involving lacto-N-biose phosphorylase in Bifidobacterium longum
Appl. Environ. Microbiol.
71
3158-3162
2005
Bifidobacterium bifidum (Q5NU16), Bifidobacterium bifidum, Bifidobacterium longum (E8MF13), Bifidobacterium longum
brenda
Nishimoto, M.; Kitaoka, M.
Identification of N-acetylhexosamine 1-kinase in the complete lacto-N-biose I/galacto-N-biose metabolic pathway in Bifidobacterium longum
Appl. Environ. Microbiol.
73
6444-6449
2007
Bifidobacterium longum subsp. Longum, Bifidobacterium longum subsp. Longum JCM 1217
brenda
Nakajima, M.; Nihira, T.; Nishimoto, M.; Kitaoka, M.
Identification of galacto-N-biose phosphorylase from Clostridium perfringens ATCC13124
Appl. Microbiol. Biotechnol.
78
465-471
2008
Bifidobacterium longum subsp. Longum, Bifidobacterium longum subsp. Longum JCM 1217, Clostridium perfringens ATCC 13124
brenda
Nishimoto, M.; Kitaoka, M.
Identification of the putative proton donor residue of lacto-N-biose phosphorylase (EC 2.4.1.211)
Biosci. Biotechnol. Biochem.
71
1587-1591
2007
Bifidobacterium bifidum JCM 1254
brenda
Nishimoto, M.; Kitaoka, M.
Practical preparation of lacto-N-biose I, a candidate for the bifidus factor in human milk
Biosci. Biotechnol. Biochem.
71
2101-2104
2007
Bifidobacterium bifidum JCM 1254
brenda
Nakajima, M.; Nishimoto, M.; Kitaoka, M.
Characterization of three beta-galactoside phosphorylases from clostridium phytofermentans: discovery of D-galactosyl-beta1,4-L-rhamnose phosphorylase
J. Biol. Chem.
284
19220-19227
2009
Lachnoclostridium phytofermentans (A9KIW5), Lachnoclostridium phytofermentans (A9KQ75), Lachnoclostridium phytofermentans
brenda
Nakajima, M.; Kitaoka, M.
Identification of lacto-N-biose I phosphorylase from Vibrio vulnificus CMCP6
Appl. Environ. Microbiol.
74
6333-6337
2008
Vibrio vulnificus (A0A3Q0KZS1), Vibrio vulnificus CMCP6LNBP (A0A3Q0KZS1)
brenda
Xiao, J.Z.; Takahashi, S.; Nishimoto, M.; Odamaki, T.; Yaeshima, T.; Iwatsuki, K.; Kitaoka, M.
Distribution of in vitro fermentation ability of lacto-N-biose I, a major building block of human milk oligosaccharides, in bifidobacterial strains
Appl. Environ. Microbiol.
76
54-59
2010
Bifidobacterium bifidum, Bifidobacterium breve, Bifidobacterium longum, no activity in Bifidobacterium adolescentis, no activity in Bifidobacterium angulatum, no activity in Bifidobacterium animalis subsp. lactis, no activity in Bifidobacterium catenulatum, no activity in Bifidobacterium dentium, no activity in Bifidobacterium pseudocatenulatum, no activity in Bifidobacterium thermophilum
brenda
Nakajima, M.; Nishimoto, M.; Kitaoka, M.
Characterization of beta-1,3-galactosyl-N-acetylhexosamine phosphorylase from Propionibacterium acnes
Appl. Microbiol. Biotechnol.
83
109-115
2009
Cutibacterium acnes (B7XEJ1), Cutibacterium acnes (B7XEJ0), Cutibacterium acnes, Cutibacterium acnes JCM 6425 (B7XEJ1), Cutibacterium acnes JCM 6473 (B7XEJ0)
brenda
Nishimoto, M.; Kitaoka, M.
One-pot enzymatic production of beta-D-galactopyranosyl-(1->3)-2-acetamido-2-deoxy-D-galactose (galacto-N-biose) from sucrose and 2-acetamido-2-deoxy-D-galactose (N-acetylgalactosamine)
Carbohydr. Res.
344
2573-2576
2009
Bifidobacterium longum, Bifidobacterium longum JCM 1217
brenda
Suzuki, R.; Wada, J.; Katayama, T.; Fushinobu, S.; Wakagi, T.; Shoun, H.; Sugimoto, H.; Tanaka, A.; Kumagai, H.; Ashida, H.; Kitaoka, M.; Yamamoto, K.
Structural and thermodynamic analyses of solute-binding protein from Bifidobacterium longum specific for core 1 disaccharide and lacto-N-biose I
J. Biol. Chem.
283
13165-13173
2008
Bifidobacterium longum (A8W790), Bifidobacterium longum, Bifidobacterium longum JCM 1217 (A8W790)
brenda
Hidaka, M.; Nishimoto, M.; Kitaoka, M.; Wakagi, T.; Shoun, H.; Fushinobu, S.
The crystal structure of galacto-N-biose/lacto-N-biose I phosphorylase: a large deformation of a TIM barrel scaffold
J. Biol. Chem.
284
7273-7283
2009
Bifidobacterium longum (E8MF13), Bifidobacterium longum
brenda
Nishimoto, M.; Hidaka, M.; Nakajima, M.; Fushinobu, S.; Kitaoka, M.
Identification of amino acid residues that determine the substrate preference of 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase
J. Mol. Catal. B
74
97-102
2012
Bifidobacterium longum (E8MF13)
-
brenda
Koyama, Y.; Hidaka, M.; Nishimoto, M.; Kitaoka, M.
Directed evolution to enhance thermostability of galacto-N-biose/lacto-N-biose I phosphorylase
Protein Eng. Des. Sel.
26
755-761
2013
Bifidobacterium longum subsp. Longum (E8MF13), Bifidobacterium longum subsp. Longum JCM 1217 (E8MF13)
brenda
Nishimoto, M.
Large scale production of lacto-N-biose I, a building block of type I human milk oligosaccharides, using sugar phosphorylases
Biosci. Biotechnol. Biochem.
84
17-24
2020
Bifidobacterium longum subsp. Longum (E8MF13), Bifidobacterium longum subsp. Longum ATCC 15707 (E8MF13)
brenda
Machida, S.; Saito, K.; Nishimoto, M.; Kitaoka, M.
Production of lacto-N-biose I using crude extracts of bifidobacterial cells
J. Appl. Glycosci. (1999)
69
15-21
2022
Bifidobacterium breve
brenda
EXTERNAL LINKS (specific for EC-Number 2.4.1.211)
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