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Information on EC 2.4.1.211 - 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase and Organism(s) Bifidobacterium longum and UniProt Accession E8MF13

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IUBMB Comments
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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This record set is specific for:
Bifidobacterium longum
UNIPROT: E8MF13
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The taxonomic range for the selected organisms is: Bifidobacterium longum
The enzyme appears in selected viruses and cellular organisms
Synonyms
glnbp, lacto-n-biose phosphorylase, galacto-n-biose/lacto-n-biose i phosphorylase, gl-bp, galacto-n-biose phosphorylase, gnb/lnb phosphorylase, beta-1,3-galactosyl-n-acetylhexosamine phosphorylase, lacto-n-biose i phosphorylase, galhexnacp, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
galacto-N-biose/lacto-N-biose I phosphorylase
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beta-D-galactopyranosyl-(1-3)-N-acetyl-D-hexosamine:phosphate galactosyltransferase
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-
-
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galacto-N-biose/lacto-N-biose I phosphorylase
-
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N-biose/lacto-N-biose I-binding protein
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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.
CAS REGISTRY NUMBER
COMMENTARY hide
224427-06-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine + phosphate
alpha-D-galactopyranose 1-phosphate + N-acetyl-D-galactosamine
show the reaction diagram
-
-
-
r
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-galactosamine
show the reaction diagram
-
-
-
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosoamine + phosphate
alpha-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
r
galacto-N-biose + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-galactosamine
show the reaction diagram
-
-
-
?
lacto-N-biose I + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
alpha-D-galactose 1-phosphate + N-acetyl-galactosamine
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosmine + phosphate
show the reaction diagram
-
-
-
-
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-galactosamine
show the reaction diagram
-
-
-
?
beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
show the reaction diagram
additional information
?
-
substrate specificity, overview. Structurally determined substrate preference for galacto-N-biose and lacto-N-biose I
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-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.72 - 24
alpha-D-galactose 1-phosphate
6.7 - 120
galacto-N-biose
2.8 - 46
lacto-N-biose I
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09 - 10.7
alpha-D-galactose 1-phosphate
3.5 - 65
galacto-N-biose
15 - 39
lacto-N-biose I
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005 - 6.21
alpha-D-galactose 1-phosphate
0.031 - 8.5
galacto-N-biose
0.34 - 9.3
lacto-N-biose I
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the GalHexNAcP belongs to the glycoside hydrolase family 112, GH112
physiological function
key enzyme for intestinal growth, phosphorolyses galacto-N-biose and lacto-N-biose I with anomeric inversion
physiological function
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GLNBP plays a key role in the colonization of bifidobacteria in the infant intestine
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
84327
x * 84327, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 84327, calculated
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
in complex with beta-D-galactopyranosyl-1,3-N-acetyl-D-glucosamine and beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D313N
mutant with undetectable activity
F364N
mutant shows severely impaired activity
N166A
mutant shows severely impaired activity
P161S
site-directed mutagenesis, the mutation leads to an increase in the selectivity on lacto-N-biose I
P161S/S336A
site-directed mutagenesis
R210E
the mutant shows no detectable activity
R32E
the mutant shows no detectable activity
R358E
the mutant shows no detectable activity
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
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)
the non-labeled enzyme is expressed in Escherichia coli BL21(DE3) cells, the selenomethionine-labeled enzyme is expressed in Escherichia coli strain B834 (DE3)
expressed in Escherichia coli B834 (DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
-
Manually annotated by BRENDA team