2.4.1.211: 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase
This is an abbreviated version!
For detailed information about 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase, go to the full flat file.
Word Map on EC 2.4.1.211
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2.4.1.211
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glutamine-binding
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longum
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ligand-free
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l-glutamine
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4-epimerase
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synthesis
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uridylyltransferase
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galnac
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bifidobacterial
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ligand-bound
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bifidus
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phosphorylases
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biotechnology
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nutrition
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medicine
- 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
Synonyms
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, cphy0577 protein, cphy3030 protein, D-galactosyl-beta1,3-N-acetyl-D-hexosamine phosphorylase, Gal-GlyNAcP, Gal-HexNAcP, 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, lnba1, lnba2, LNBP, lnpA, N-biose/lacto-N-biose I-binding protein
ECTree
2.4.1.211 1,3-beta-galactosyl-N-acetylhexosamine phosphorylaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.4.1.211 - 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase
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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
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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
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D576A
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random mutagenesis, the mutant shows highly increased thermostability compared to the wild-type
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D576V
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random mutagenesis, the mutant shows highly increased thermostability compared to the wild-type
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R290H
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random mutagenesis, the mutant shows slightly increased thermostability and slightly reduced activity compared to the wild-type
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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
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enzyme engineering for improved thermostability, random mutagenesis GLNBP library construction using error-prone polymerase chain reaction and mutant screening, overview
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