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Information on EC 2.4.1.211 - 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase and Organism(s) Cutibacterium acnes and UniProt Accession B7XEJ1

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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:
Cutibacterium acnes
UNIPROT: B7XEJ1
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The taxonomic range for the selected organisms is: Cutibacterium acnes
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, gnb/lnb phosphorylase, beta-1,3-galactosyl-n-acetylhexosamine phosphorylase, galacto-n-biose phosphorylase, lacto-n-biose i phosphorylase, galhexnacp, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-1,3-galactosyl-N-acetylhexosamine phosphorylase
-
galacto-N-biose phosphorylase
-
beta-1,3-galactosyl-N-acetylhexosamine phosphorylase
-
beta-D-galactopyranosyl-(1-3)-N-acetyl-D-hexosamine:phosphate galactosyltransferase
-
-
-
-
galacto-N-biose phosphorylase
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
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
-
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-galactose 1-phosphate + N-acetyl-D-galactosamine
show the reaction diagram
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
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-glucosamine + phosphate
alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine
show the reaction diagram
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
-
-
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
-
-
-
?
additional information
?
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
140
beta-D-galactopyranosyl-1,3-N-acetyl-D-galactosamine
in 100 mM MOPS buffer (pH 7.0) at 37°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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain JCM6425
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
B7XEJ1_CUTAC
738
0
82140
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80000
His-tagged enzyme, SDS-PAGE
83480
His-tagged enzyme, calculated from amino acid sequence
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
-
701840
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
the enzyme is stable up to 37°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (B7XEJ0), Cutibacterium acnes (B7XEJ1), Cutibacterium acnes, Cutibacterium acnes JCM 6425 (B7XEJ1), Cutibacterium acnes JCM 6473 (B7XEJ0)
Manually annotated by BRENDA team