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CTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + CDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
diphosphate + UDP-glucose
UTP + D-glucose 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
N-acetyl-4-deoxy-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-4-deoxy-alpha-D-glucosamine + diphosphate
-
-
yield: 59%
-
?
N-acetyl-6-deoxy-6-azido-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-6-deoxy-6-azido-alpha-D-glucosamine + diphosphate
-
-
yield: 20%
-
?
N-acetyl-6-deoxy-alpha-D-galactosamine 1-phosphate + UTP
UDP-N-acetyl-6-deoxy-alpha-D-galactosamine + diphosphate
-
-
yield: 55%
-
?
N-acetyl-6-deoxy-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-6-deoxy-alpha-D-glucosamine + diphosphate
-
-
yield: 50%
-
?
N-acetyl-alpha-D-allopyranosylamine 1-phosphate + UTP
UDP-N-acetyl-alpha-D-allopyranosylamine + diphosphate
-
-
yield: 20%
-
?
N-acetyl-alpha-D-galactosamine 1-phosphate + UTP
UDP-N-acetyl-alpha-D-galactosamine + diphosphate
-
-
yield: 65%
-
?
N-acetyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-alpha-D-glucosamine + diphosphate
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-D-glucosamine + diphosphate
N-acetylglucosamine 1-phosphate + uridine 5'-triphosphate
uridine-diphospho-N-acetylglucosamine + diphosphate
-
-
-
-
r
N-azidoacetyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-azidoacetyl-alpha-D-glucosamine + diphosphate
-
-
yield: 44%
-
?
N-butanoyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-butanoyl-alpha-D-glucosamine + diphosphate
-
-
yield: 27%
-
?
N-propanoyl-alpha-D-galactosamine 1-phosphate + UTP
UDP-N-propanoyl-alpha-D-galactosamine + diphosphate
-
-
yield: 10%
-
?
N-propanoyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-propanoyl-alpha-D-glucosamine + diphosphate
-
-
yield: 57%
-
?
UDP-N-acetyl-D-galactosamine + diphosphate
N-acetyl-D-galactosamine 1-phosphate + UTP
-
-
-
r
UDP-N-acetyl-D-glucosamine + diphosphate
N-acetyl-D-glucosamine 1-phosphate + UTP
-
-
-
r
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
UTP + GalNAzMe-1-phosphate
diphosphate + UDP-GalNAzMe
the reaction is catalyzed only by mutant F383A
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-galactosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetylglucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
-
-
-
?
additional information
?
-
diphosphate + UDP-glucose
UTP + D-glucose 1-phosphate
-
30% of the activity with UDP-N-acetylglucosamine
-
-
?
diphosphate + UDP-glucose
UTP + D-glucose 1-phosphate
-
-
-
r
diphosphate + UDP-glucose
UTP + D-glucose 1-phosphate
-
-
-
-
?
diphosphate + UDP-glucose
UTP + D-glucose 1-phosphate
-
-
-
-
r
diphosphate + UDP-glucose
UTP + D-glucose 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
-
?
diphosphate + UDP-N-acetyl-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
2-3 times more active with N-acetyl-D-galactosamine 1-phosphate than with N-acetyl-D-glucosamine 1-phosphate, AGX2 8 times less active with N-acetyl-D-galactosamine 1-phosphate than with N-acetyl-D-glucosamine 1-phosphate
-
-
?
diphosphate + UDP-N-acetyl-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
2.8% of the activity with UDP-N-acetylglucosamine
-
-
?
diphosphate + UDP-N-acetyl-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-galactosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
the reaction proceeds as an SN2 reaction
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
enzyme of the Leloir pathway
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
key enzyme of encystment
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
highly specific, no activity with any other sugar nucloetide tested
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and teichoic acid
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
highly specific, no activity with any other sugar nucloetide tested
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
highly specific, no activity with any other sugar nucloetide tested
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and teichoic acid
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
deficiency mutant fully swollen and some are lysed
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
-
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in formation of N-linked oligosaccharides
-
r
N-acetyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-alpha-D-glucosamine + diphosphate
-
-
yield: 40%
-
?
N-acetyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-alpha-D-glucosamine + diphosphate
-
-
-
?
N-acetyl-alpha-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-alpha-D-glucosamine + diphosphate
-
-
-
?
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-D-glucosamine + diphosphate
-
-
-
r
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-D-glucosamine + diphosphate
-
-
-
-
?
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-D-glucosamine + diphosphate
-
-
-
?
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-D-glucosamine + diphosphate
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
the activity with N-acetyl-D-glucosamine-1-phosphate is 3.4 times higher, respectively, than the corresponding activity with alpha-D-glucose-1-phosphate
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
the activity with N-acetyl-D-glucosamine-1-phosphate is 3.4 times higher, respectively, than the corresponding activity with alpha-D-glucose-1-phosphate
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
-
-
-
?
UTP + alpha-D-glucose 1-phosphate
diphosphate + UDP-alpha-D-glucose
-
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
reaction of EC 2.7.7.83
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
reaction of EC 2.7.7.83
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
reaction of EC 2.7.7.83
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
reaction of EC 2.7.7.83
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
reaction of EC 2.7.7.83
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
reaction of EC 2.7.7.83
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-galactosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-galactosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?, r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
KT282116, KT282117
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
because the multifunctional ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
the enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
the enzyme also shows activity of EC 2.7.7.24, glucose-1-phosphate thymidylyltransferase
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
the multifunctional enzyme also shows activity with UTP + alpha-D-glucose 1-phosphate (EC 2.7.7.9, UTP-glucose-1-phosphate uridylyltransferase), UTP + N-acetylglucosamine 1-phosphate (EC 2.7.7.24, glucose-1-phosphate thymidylyltransferase), dTTP + N-acetylglucosamine 1-phosphate (N-acetylglucosamine 1-phosphate thymidylyltransferase), dCTP + alpha-D-glucose 1-phosphate (glucose-1-phosphate cytidylyltransferase), dGTP + alpha-D-glucose 1-phosphate (glucose-1-phosphate guanylyltransferase), dATP + alpha-D-glucose 1-phosphate (glucose-1-phosphate adenylyltransferase). No activity with: alpha-D-glucose 1-phosphate + dATP, alpha-D-glucose 1-phosphate + dCTP, alpha-D-glucose 1-phosphate + dGTP, UTP + alpha-D-mannose1-phosphate, UTP + alpha-D-galactose 1-phosphate, UTP + alpha-D-glucosamine 1-phosphate
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
the enzyme is involved in biosyntheis of UDP-N-acetylglusosamine
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
the activity with N-acetyl-D-glucosamine-1-phosphate is 3.4 times higher, respectively, than the corresponding activity with alpha-D-glucose-1-phosphate
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
because the multifunctional ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
the multifunctional enzyme also shows activity with UTP + alpha-D-glucose 1-phosphate (EC 2.7.7.9, UTP-glucose-1-phosphate uridylyltransferase), UTP + N-acetylglucosamine 1-phosphate (EC 2.7.7.24, glucose-1-phosphate thymidylyltransferase), dTTP + N-acetylglucosamine 1-phosphate (N-acetylglucosamine 1-phosphate thymidylyltransferase), dCTP + alpha-D-glucose 1-phosphate (glucose-1-phosphate cytidylyltransferase), dGTP + alpha-D-glucose 1-phosphate (glucose-1-phosphate guanylyltransferase), dATP + alpha-D-glucose 1-phosphate (glucose-1-phosphate adenylyltransferase). No activity with: alpha-D-glucose 1-phosphate + dATP, alpha-D-glucose 1-phosphate + dCTP, alpha-D-glucose 1-phosphate + dGTP, UTP + alpha-D-mannose1-phosphate, UTP + alpha-D-galactose 1-phosphate, UTP + alpha-D-glucosamine 1-phosphate
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
the enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
the enzyme also shows activity of EC 2.7.7.24, glucose-1-phosphate thymidylyltransferase
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
the enzyme is involved in biosyntheis of UDP-N-acetylglusosamine
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
the activity with N-acetyl-D-glucosamine-1-phosphate is 3.4 times higher, respectively, than the corresponding activity with alpha-D-glucose-1-phosphate
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
involved in the synthesis of UDP-N-acetyl-galactoseamine, which is important for cyst wall synthesis
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
involved in the synthesis of UDP-N-acetyl-galactoseamine, which is required for cyst wall synthesis
-
-
?
additional information
?
-
enzyme additionally shows the activity of UTP-glucose-1-phosphate uridylyltransferase, EC 2.7.7.9
-
-
?
additional information
?
-
enzyme additionally shows the activity of UTP-glucose-1-phosphate uridylyltransferase, EC 2.7.7.9
-
-
?
additional information
?
-
no substrates: CTP, GTP, ITP or ATP, glucose 1-phosphate, glucosamine 1-phosphate, xylose 1-phosphate, galactose 1-phosphate, galactosamin 1-phosphate, fucose 1-phosphate, mannose 1-phosphate, galactosamine 1-phosphate, fructose 1-phosphate, or glucose 6-phosphate
-
-
?
additional information
?
-
no substrates: CTP, GTP, ITP or ATP, glucose 1-phosphate, glucosamine 1-phosphate, xylose 1-phosphate, galactose 1-phosphate, galactosamin 1-phosphate, fucose 1-phosphate, mannose 1-phosphate, galactosamine 1-phosphate, fructose 1-phosphate, or glucose 6-phosphate
-
-
?
additional information
?
-
GlcNAc-1-P displays hydrogen bond interactions with residues Q110, R113, K120, D209, S215, and A217. the loops moved close to UTP and narrowed the entrance. Other residues that are surrounding the UTP include L106, G108, G109, K120, P218, D219, G220, N325, I326, C327, K374, and F378, which form hydrophobic, electrostatic, and van der Waals interactions, thus increasing the stability of this complex. In UTP-bound form, the residues present in the nucleotide-binding loop of UAP does not have a major role in binding to uridine. Docking analysis of substrates and products, overview
-
-
-
additional information
?
-
-
GlcNAc-1-P displays hydrogen bond interactions with residues Q110, R113, K120, D209, S215, and A217. the loops moved close to UTP and narrowed the entrance. Other residues that are surrounding the UTP include L106, G108, G109, K120, P218, D219, G220, N325, I326, C327, K374, and F378, which form hydrophobic, electrostatic, and van der Waals interactions, thus increasing the stability of this complex. In UTP-bound form, the residues present in the nucleotide-binding loop of UAP does not have a major role in binding to uridine. Docking analysis of substrates and products, overview
-
-
-
additional information
?
-
-
glycosylation pathway
-
-
?
additional information
?
-
-
enzyme shows relaxed tolerance for modifications at N-acyl, C-3, C-4, and C-6 positions, with a preference for small substituent groups. The yields are low to moderate (10-65%) and some sugar-1-Ps fail to generate the corresponding UDP-sugars due to the steric problem
-
-
?
additional information
?
-
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. Acetyltransfer precedes uridyltransfer with both the acetyltransferase and uridyltransferase reactions taking place in two separable active sites in bifunctional GlmU where the acetyltransferase domain of GlmU does not show homology with its eukaryotic counterpart
-
-
?
additional information
?
-
the uridyltransferase domain of GlmU exhibits a flexible substrate specificity, roles of several highly conserved amino acid residues involved in substrate binding and recognition, overview. Besides UTP, the enzyme also shows activity with CTP, ATP, and slightly with dATP
-
-
?
additional information
?
-
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. Acetyltransfer precedes uridyltransfer with both the acetyltransferase and uridyltransferase reactions taking place in two separable active sites in bifunctional GlmU where the acetyltransferase domain of GlmU does not show homology with its eukaryotic counterpart
-
-
?
additional information
?
-
the human and trypanosome enzymes both display a strictly ordered bi-bi mechanism, but with the order of substrate binding reversed. Human UAP does not bind UTP alone, and although it does show significant binding to GlcNAc-1-P, it is not possible to calculate an affinity due to complex binding kinetics
-
-
?
additional information
?
-
-
the human and trypanosome enzymes both display a strictly ordered bi-bi mechanism, but with the order of substrate binding reversed. Human UAP does not bind UTP alone, and although it does show significant binding to GlcNAc-1-P, it is not possible to calculate an affinity due to complex binding kinetics
-
-
?
additional information
?
-
-
the molecular recognition of the enzyme with the substrates occurs mainly by hydrogen bonds between ligands and Arg116, Arg383, Gly381, and Lys408 amino acids, and few hydrophobic interactions with Tyr382 and Lys123 residues
-
-
?
additional information
?
-
the molecular recognition of the enzyme with the substrates occurs mainly by hydrogen bonds between ligands and Arg116, Arg383, Gly381, and Lys408 amino acids, and few hydrophobic interactions with Tyr382 and Lys123 residues
-
-
?
additional information
?
-
-
bifunctional enzyme that catalyzes two consecutive reactions leading to the biosynthesis of UDP-N-acetylglucosamine, in the first reaction, GlmU catalyzes the CoA-dependent acetylation of glucosamine-1-phosphate to afford N-acetylglucosamine-1-phosphate, in the second reaction, the UMP moiety from a UTP molecule is transferred to N-acetyl-alpha-D-glucosamine 1-phosphate to give the final product UDP-GlcNAc
-
-
?
additional information
?
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase, the enzyme catalyzes the two reactions, acetyl transfer and uridyl transfer, at two independent domains, regulation, overview
-
-
?
additional information
?
-
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase, the enzyme catalyzes the two reactions, acetyl transfer and uridyl transfer, at two independent domains, regulation, overview
-
-
?
additional information
?
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively
-
-
?
additional information
?
-
the bifunctional role of GlmU arises from two independent domains of the enzyme which possess acetyltransferase, EC 2.3.1.157, and uridyltransferase, EC 2.7.7.23, activities. The acetyltransferase domain, found in the C-terminus of the protein, is responsible for the first step of the reaction, in which an acetyl group is transferred from AcCoA to GlcN-1-P forming GlcNAc-1-P. GlcNAc-1-P then serves as a substrate for the uridyltransferase active site in the N-terminus of the enzyme which forms UDP-GlcNAc
-
-
?
additional information
?
-
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols
-
-
?
additional information
?
-
-
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols
-
-
?
additional information
?
-
coupled assay method: coupling of the two enzyme reactions via N-acetyl-alpha-D-glucosamine 1-phosphate for determination of the acetyl transferase activity of the enzyme
-
-
?
additional information
?
-
-
coupled assay method: coupling of the two enzyme reactions via N-acetyl-alpha-D-glucosamine 1-phosphate for determination of the acetyl transferase activity of the enzyme
-
-
?
additional information
?
-
development of a double-enzyme-coupled continuous assay for Mycobacterium tuberculosis GlmU uridyltransferase. The assay used excess amounts of two coupling enzymes, namely inorganic pyrophosphatase (IPP) (EC 3.6.1.1) and purine nucleoside phosphorylase (PNPase) (EC 2.4.2.1) in the presence of 2-amino-6-mercapto-7-methylpurine ribonucleoside. the pyrophosphate produced by GlmU uridyltransferase is subsequently hydrolysed to phosphate by IPP. The phosphate then serves as a substrate for PNPase which catalyses the phosphorolytic cleavage of the glycosidic bond in 2-amino-6-mercapto-7-methylpurine ribonucleoside, resulting in the formation of 2-amino-6-mercapto-7-methylpurine that can be detected spectroscopically
-
-
?
additional information
?
-
-
enzyme GlmU is specific for its natural substrates UTP and N-acetyl-alpha-D-glucosamine 1-phosphate, substrate specificity, overview. No activity with ATP and TTP as well as glucose-1-phosphate and mannose-1-phosphate, very poor activity with GTP, low activity with CTP
-
-
?
additional information
?
-
the recombinant enzyme binds to human interleukin-8, interaction analysis with human neutrophils, overview
-
-
?
additional information
?
-
-
the recombinant enzyme binds to human interleukin-8, interaction analysis with human neutrophils, overview
-
-
?
additional information
?
-
-
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols
-
-
?
additional information
?
-
-
bifunctional enzyme that catalyzes two consecutive reactions leading to the biosynthesis of UDP-N-acetylglucosamine, in the first reaction, GlmU catalyzes the CoA-dependent acetylation of glucosamine-1-phosphate to afford N-acetylglucosamine-1-phosphate, in the second reaction, the UMP moiety from a UTP molecule is transferred to N-acetyl-alpha-D-glucosamine 1-phosphate to give the final product UDP-GlcNAc
-
-
?
additional information
?
-
the recombinant enzyme binds to human interleukin-8, interaction analysis with human neutrophils, overview
-
-
?
additional information
?
-
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols
-
-
?
additional information
?
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively
-
-
?
additional information
?
-
the bifunctional role of GlmU arises from two independent domains of the enzyme which possess acetyltransferase, EC 2.3.1.157, and uridyltransferase, EC 2.7.7.23, activities. The acetyltransferase domain, found in the C-terminus of the protein, is responsible for the first step of the reaction, in which an acetyl group is transferred from AcCoA to GlcN-1-P forming GlcNAc-1-P. GlcNAc-1-P then serves as a substrate for the uridyltransferase active site in the N-terminus of the enzyme which forms UDP-GlcNAc
-
-
?
additional information
?
-
development of a double-enzyme-coupled continuous assay for Mycobacterium tuberculosis GlmU uridyltransferase. The assay used excess amounts of two coupling enzymes, namely inorganic pyrophosphatase (IPP) (EC 3.6.1.1) and purine nucleoside phosphorylase (PNPase) (EC 2.4.2.1) in the presence of 2-amino-6-mercapto-7-methylpurine ribonucleoside. the pyrophosphate produced by GlmU uridyltransferase is subsequently hydrolysed to phosphate by IPP. The phosphate then serves as a substrate for PNPase which catalyses the phosphorolytic cleavage of the glycosidic bond in 2-amino-6-mercapto-7-methylpurine ribonucleoside, resulting in the formation of 2-amino-6-mercapto-7-methylpurine that can be detected spectroscopically
-
-
?
additional information
?
-
the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity
-
-
?
additional information
?
-
-
the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity
-
-
?
additional information
?
-
-
the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity
-
-
?
additional information
?
-
the enzyme has multiple sugar-1-phosphate nucleotidylyltransferase, EC 2.7.7.37, and amino-sugar-1-phosphate acetyltransferase, EC 2.3.1.157, activities, overview. In addition to glucosamine-1-phosphate acetyltransferase activity, it possesses unique galactosamine-1-phosphate acetyltransferase activity. Also, the enzyme possesses GlcNAc-1-phosphate nucleotidylyltransferase, EC 2.7.7.23, and N-acetyl-D-galactosamine-1-phosphate uridyltransferase, EC 2.7.7.83, activities, as well as the expected glucose-1-phosphate thymidylyltransferase, EC 2.7.7.24, activity
-
-
?
additional information
?
-
the human and trypanosome enzymes both display a strictly ordered bi-bi mechanism, but with the order of substrate binding reversed. Trypanosoma brucei UAP binds UTP alone with a KD of 83.1 microM, but does not bind GlcNAc-1-P alone
-
-
?
additional information
?
-
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
the human and trypanosome enzymes both display a strictly ordered bi-bi mechanism, but with the order of substrate binding reversed. Trypanosoma brucei UAP binds UTP alone with a KD of 83.1 microM, but does not bind GlcNAc-1-P alone
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
N-acetyl-D-glucosamine 1-phosphate + UTP
UDP-N-acetyl-D-glucosamine + diphosphate
-
-
-
-
?
N-acetylglucosamine 1-phosphate + uridine 5'-triphosphate
uridine-diphospho-N-acetylglucosamine + diphosphate
-
-
-
-
r
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
additional information
?
-
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
enzyme of the Leloir pathway
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
key enzyme of encystment
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and teichoic acid
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in synthesis of peptidoglycan and teichoic acid
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
involved in the interconversion of various amino sugars and in the synthesis of mucopolysaccharides, glycopeptides, chitin
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
deficiency mutant fully swollen and some are lysed
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
involved in synthesis of peptidoglycan and lipopolysaccharide
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
amino sugar metabolism
-
r
diphosphate + UDP-N-acetyl-D-glucosamine
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
involved in formation of N-linked oligosaccharides
-
r
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
reaction of EC 2.7.7.83
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
-
-
-
r
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
reaction of EC 2.7.7.83
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
reaction of EC 2.7.7.83
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
reaction of EC 2.7.7.83
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
reaction of EC 2.7.7.83
-
-
?
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
reaction of EC 2.7.7.83
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?, r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
KT282116, KT282117
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
because the multifunctional ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
the enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
the enzyme is involved in biosyntheis of UDP-N-acetylglusosamine
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
because the multifunctional ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
the enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
the enzyme is involved in biosyntheis of UDP-N-acetylglusosamine
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
involved in the synthesis of UDP-N-acetyl-galactoseamine, which is important for cyst wall synthesis
-
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
diphosphate + UDP-N-acetyl-D-glucosamine
involved in the synthesis of UDP-N-acetyl-galactoseamine, which is required for cyst wall synthesis
-
-
?
additional information
?
-
-
glycosylation pathway
-
-
?
additional information
?
-
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. Acetyltransfer precedes uridyltransfer with both the acetyltransferase and uridyltransferase reactions taking place in two separable active sites in bifunctional GlmU where the acetyltransferase domain of GlmU does not show homology with its eukaryotic counterpart
-
-
?
additional information
?
-
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. Acetyltransfer precedes uridyltransfer with both the acetyltransferase and uridyltransferase reactions taking place in two separable active sites in bifunctional GlmU where the acetyltransferase domain of GlmU does not show homology with its eukaryotic counterpart
-
-
?
additional information
?
-
-
bifunctional enzyme that catalyzes two consecutive reactions leading to the biosynthesis of UDP-N-acetylglucosamine, in the first reaction, GlmU catalyzes the CoA-dependent acetylation of glucosamine-1-phosphate to afford N-acetylglucosamine-1-phosphate, in the second reaction, the UMP moiety from a UTP molecule is transferred to N-acetyl-alpha-D-glucosamine 1-phosphate to give the final product UDP-GlcNAc
-
-
?
additional information
?
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase, the enzyme catalyzes the two reactions, acetyl transfer and uridyl transfer, at two independent domains, regulation, overview
-
-
?
additional information
?
-
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase, the enzyme catalyzes the two reactions, acetyl transfer and uridyl transfer, at two independent domains, regulation, overview
-
-
?
additional information
?
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively
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-
?
additional information
?
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the bifunctional role of GlmU arises from two independent domains of the enzyme which possess acetyltransferase, EC 2.3.1.157, and uridyltransferase, EC 2.7.7.23, activities. The acetyltransferase domain, found in the C-terminus of the protein, is responsible for the first step of the reaction, in which an acetyl group is transferred from AcCoA to GlcN-1-P forming GlcNAc-1-P. GlcNAc-1-P then serves as a substrate for the uridyltransferase active site in the N-terminus of the enzyme which forms UDP-GlcNAc
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-
?
additional information
?
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the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols
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?
additional information
?
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the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols
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?
additional information
?
-
-
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols
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additional information
?
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bifunctional enzyme that catalyzes two consecutive reactions leading to the biosynthesis of UDP-N-acetylglucosamine, in the first reaction, GlmU catalyzes the CoA-dependent acetylation of glucosamine-1-phosphate to afford N-acetylglucosamine-1-phosphate, in the second reaction, the UMP moiety from a UTP molecule is transferred to N-acetyl-alpha-D-glucosamine 1-phosphate to give the final product UDP-GlcNAc
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-
?
additional information
?
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the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols
-
-
?
additional information
?
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively
-
-
?
additional information
?
-
the bifunctional role of GlmU arises from two independent domains of the enzyme which possess acetyltransferase, EC 2.3.1.157, and uridyltransferase, EC 2.7.7.23, activities. The acetyltransferase domain, found in the C-terminus of the protein, is responsible for the first step of the reaction, in which an acetyl group is transferred from AcCoA to GlcN-1-P forming GlcNAc-1-P. GlcNAc-1-P then serves as a substrate for the uridyltransferase active site in the N-terminus of the enzyme which forms UDP-GlcNAc
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?
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(2S,4R)-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-4-hydroxypyrrolidine-2-carboxamide
-
(3-hydroxyphenyl)[4-(5,6,7,8-tetrahydroquinazolin-4-ylamino)phenyl]methanone
30% inhibition at 0.05 mM
(4-(6,7-dimethoxyquinazolin-4-yl)piperazin-1-yl)(phenyl)-methanone
-
-
(S)-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)pyrrolidine-2-carboxamide
-
(Z)-4-(4-(benzyloxy)benzylidene)-2-(naphthalen-1-yl)oxazol-5(4H)-one
i.e. Oxa33, synthesis of a specific GlmU inhibitor, molecular docking study, the inhibitor binds to an allosteric site of the uridyltransferase domain, overview. Oxa33 fails to inhibit cell growth even at concentrations as high as 0.150 mM. Tyr150, Glu250 and Arg 253 are in hydrogen bonding with carbonyl oxygen over the oxazole ring, while Leu144, Pro147, Phe148, Tyr150, Ala233, Ala236 and Leu247 participate in strong hydrophobic interactions with Oxa33
1-(3-hydroxybenzoyl)-4-(thieno[3,2-d]pyrimidin-4-ylamino)pyridinium
38% inhibition at 0.05 mM
1-[(2S,3S,4R,5S)-3,4-dihydroxy-5-(hydroxymethyl)tetrahydrofuran-2-yl]dihydropyrimidine-2,4(1H,3H)-dione
1-[2,4-dimethoxy-5-(10H-phenoxazin-10-ylsulfonyl) phenylamino]-2-(-4-pyridyl)-1-ethanone
commercial inhibitor
2,3-dihydroxy-5-nitrophenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside
forms with UNAcP hydrogen bonds, Pi-cation and hydrophobic interactions
2-(3-((4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)carbamoyl)phenoxy)acetic acid
34% inhibition at 0.05 mM
2-2-[(6-nitroquinazolin-4-yl)amino]ethoxy)-ethan-1-ol
-
2-amino-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-benzamide
16% inhibition at 0.05 mM
2-hydroxy-5-nitrophenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside
-
2-hydroxyphenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside
-
2-[2-[(6-nitroquinazolin-4-yl)amino]ethoxy]-ethan-1-ol
-
3,4-dihydroxyphenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside
-
3-(cyanomethoxy)-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)-phenyl)benzamide
-
3-amino-N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-benzamide
17% inhibition at 0.05 mM
3-hydroxyphenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside
-
3-nitrophenyl 2-acetamido-2-deoxy-alpha-D-xylo-hexopyranoside
-
3-[(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)oxy]-2-hydroxy-N-[2-[(3-hydroxypropyl)carbamoyl]phenyl]benzamide
-
3-[2-(1,3-benzodioxol-5-yl)-2-oxoethyl]-4-bromo-3-hydroxy-5-methyl-1,3-dihydro-2H-indol-2-one
competitive inhibitor with selectivity over the human counterpart, binds at an allosteric site absent in the human homologue that prevents the conformational rearrangement required to bind UTP
3-[2-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-oxoethyl]-3-hydroxy-5-methyl-1,3-dihydro-2H-indol-2-one
-
-
3-[2-(2H-1,3-benzodioxol-5-yl)-2-oxoethyl]-3-hydroxy-6,7-dimethyl-1,3-dihydro-2H-indol-2-one
-
-
3-[2-(2H-1,3-benzodioxol-5-yl)-2-oxoethyl]-3-hydroxy-7-methyl-1,3-dihydro-2H-indol-2-one
-
-
3-[2-(2H-1,3-benzodioxol-5-yl)-2-oxoethyl]-4,6-dichloro-3-hydroxy-1,3-dihydro-2H-indol-2-one
-
-
3-[2H-(1,3-benzodioxol-5-yl)-2-oxoethyl]-4-bromo-3-hydroxy-5-methyl-1,3-dihydro-2H-indol-2-one
-
UTP-competitive inhibitor with selectivity over the human counterpart despite the high level of conservation of active site residues. The inhibitor binds at an allosteric site
3-[[2-acetamido-2-deoxy-alpha-D-xylo-hexopyranosyl]oxy]-2-hydroxybenzoic acid
-
3-[[2-acetamido-2-deoxy-alpha-L-xylo-hexopyranosyl]oxy]benzoic acid
-
4-(5-[(6-nitroquinazolin-4-yl)amino]-1,3,4-thiadiazol-2-yl)phenol
-
4-(6-nitroquinazolin-4-ylamino)benzoic acid
-
4-chloro-N-(3-methoxypropyl)-N-[1-(2-phenylethyl)piperidin-3-yl]benzamide
a 1.9 A resolution crystal structure of this synthetic small-molecule inhibitor of GlmU is presented. The determined crystal structure indicates that the inhibitor occupies an allosteric site adjacent to the GlcNAc-1-P substrate-binding region, thus, preventing structural rearrangements that are required for the enzymatic reaction
4-chloro-N-[1-[2-(2-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide
-
4-chloro-N-[1-[2-(3-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide
-
4-chloro-N-[1-[2-(4-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide
-
4-fluoro-N-(3-methoxypropyl)-N-[1-(2-phenylethyl)piperidin-3-yl]benzamide
-
4-methyl-7-[(6-nitroquinazolin-4-yl)amino]-2H-1-benzopyran-2-one
-
4-[(6-nitroquinazolin-4-yl)amino]-N-(pyrimidin-2-yl)benzene-1-sulfonamide
-
4-[5-[(6-nitroquinazolin-4-yl)amino]-1,3,4-thiadiazol-2-yl]phenol
-
5'-(3-[[2-acetamido-2-deoxy-alpha-L-xylo-hexopyranosyl]oxy]-2-hydroxyanilino)-5'-deoxyuridine
-
5'-deoxy-5'-[[4-(3,4-dihydroxyphenyl)-1,3-thiazol-2-yl]amino]uridine
37% inhibition at 2 mM
5'-[N-[2-[[2-(acetylamino)-2-deoxy-D-glucopyranosyl]oxy]acetyl]sulfamoyl]uridine
55% inhibition at 2 mM
5'-[[2-(cyclohexylamino)-2-oxoethyl](2,3-dihydroxybenzoyl)amino]-5'-deoxyuridine
10% inhibition at 2 mM
5'-[[N-[2-[[2-(acetylamino)-2-deoxy-alpha-D-glucopyranosyl]oxy]acetyl]-L-alpha-aspartyl-L-alpha-aspartyl]amino]-5'-deoxyuridine
60% inhibition at 2 mM
6,7-dimethoxy-4-(piperazin-1-yl)quinazoline
-
6-nitro-N-(1,3-thiazol-2-yl)quinazolin-4-amine
-
6-nitro-N-(3,4,5-trimethoxyphenyl)quinazolin-4-amine
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6-nitro-N-(5-phenyl-1,3,4-thiadiazol-2-yl)quinazolin-4-amine
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6-nitro-N-(pyridin-2-ylmethyl)quinazolin-4-amine
-
6-nitro-N-[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]quinazolin-4-amine
-
6-nitro-N-[5-(trifluoromethyl)-1,3,4-thiadiazol-2-yl]quinazolin-4-amine
-
9H-fluoren-9-ylmethyl (2S)-2-([4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl]carbamoyl)pyrrolidine-1-carboxylate
-
9H-fluoren-9-ylmethyl (2S)-2-[(4-aminophenyl)carbamoyl]pyrrolidine-1-carboxylate
-
ATP
-
the enzyme binds three magnesium ions and ATP at the active site, but shows no activity with ATP. ATP binding results in an inactive pre-catalytic enzymesubstrate complex, where it adopts an unusual conformation such that the reaction cannot be catalyzed
cyclohexyl(4-(6,7-dimethoxyquinazolin-4-yl)piperazin-1-yl)-methanone
-
hygromycin
0.5 mg/ml, 36% reduction in activity
luteolin
minimal inhibitory concentration for growth of Xanthomonas oryzae pv. oryzae, 186 microg/ml
N'-[(4-chloro-3,5-dimethylphenoxy)acetyl]-2,4-dihydroxybenzohydrazide
minimal inhibitory concentration for growth of Xanthomonas oryzae pv. oryzae, 420 microg/ml
N'1,N'6-bis[2-(naphthalen-2-yloxy)acetyl]hexanedihydrazide
minimal inhibitory concentration for growth of Xanthomonas oryzae pv. oryzae, 302 microg/ml
N-(1-benzylpiperidin-4-yl)-6-nitroquinazolin-4-amine
-
N-(2,4-dimethylphenyl)-6-nitroquinazolin-4-amine
-
N-(2-((6,7-dimethoxyquinazolin-4-yl)amino)cyclohexyl)benzamide
-
N-(2-((6,7-dimethoxyquinazolin-4-yl)amino)cyclohexyl)cyclohexane carboxamide
-
N-(3,5-dimethoxyphenyl)-2,3-dihydro-4H-1,4-benzothiazine-4-carboxamide
-
-
N-(3-methylpiperazin-1-yl)-6-nitroquinazolin-4-amine
-
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-2-hydroxybenzamide
14% inhibition at 0.05 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-2-nitrobenzamide
13% inhibition at 0.05 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-3-(4-fluoro-phenyl)-5-methylisoxazole-4-carboxamide
19% inhibition at 0.05 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-3-hydroxybenzamide
35% inhibition at 0.05 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-3-methoxy benzamide
38% inhibition at 0.05 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-3-nitrobenzamide
-
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-4-fluorobenzamide
21% inhibition at 0.05 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-4-hydroxybenzamide
18% inhibition at 0.05 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)cyclohexane carboxamide
22% inhibition at 2 mM
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)pyrazine-2-carboxamide
19% inhibition at 0.05 mM
N-(4-[(6-nitroquinazolin-4-yl)amino]benzene-1-sulfonyl)acetamide
-
N-(5-methyl-1,3,4-thiadiazol-2-yl)-6-nitroquinazolin-4-amine
-
N-carbamimidoyl-4-[(6-nitroquinazolin-4-yl)-amino]benzene-1-sulfonamide
compound with sulfaguanidine moiety at 4th position of quinazoline forms polar hydrogen bond with Glu 166 and Gln 205 via guanidine moiety. Lys 26 forms pi-pi stacking with the phenyl ring of sulfaguanidine and hydrogen bonding with the nitro functional g
N-cyclohexyl-6-nitroquinazolin-4-amine
-
N-cyclopropyl-6-nitroquinazolin-4-amine
-
N-[(1R,2R,4R,6S)-6-(2,3-dihydroxy-5-nitrophenoxy)-2,3-dihydroxy-4-(hydroxymethyl)cyclohexyl]acetamide
inhibitor identified by strucutre-based drug design, best binding energy of ?95.2 kcal/mol among the compounds analyzed
N-[(2R,3R,4R,6R)-2-(2,3-dihydroxy-5-nitrophenoxy)-4,5-dihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-3-yl]acetamide
most active inhibitor among compounds tested, forms a hydrogen bonding network with residues Arg116, Gly381, Arg383 and Lys408, with the distance ranging from 2.9 A to and 3.14 A. The hydrophobic interaction is observed with the aromatic ring of Tyr382 with a distance of 3.85 A. The aromatic ring of the inhibitor also interacts with the Lys123 through a pi-cation interaction, with a distance of 3.99 A
N-[4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl]-3-methoxybenzamide
38% inhibition; 38% inhibition at 0.05 mM
N-[4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl]benzamide
N-[4-[(6-nitroquinazolin-4-yl)amino]benzene-1-sulfonyl]acetamide
-
N-[4-[(7-hydroxy-6-methoxyquinazolin-4-yl)amino]phenyl]benzamide
N-[5-(2-chlorophenyl)-1,3,4-thiadiazol-2-yl]-6-nitroquinazolin-4-amine
-
N1',N3'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide
-
-
N1',N3'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide
-
-
N1',N3'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide
-
-
N1',N3'-bis(2-(naphthalen-2-yloxy)acetyl) isophthalohydrazide
-
-
N1',N4'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide
-
-
N1',N4'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide
-
-
N1',N4'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide
-
-
N1',N4'-bis(2-(naphthalen-2-yloxy)acetyl) succinohydrazide
-
-
N1',N6'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide
-
-
N1',N6'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide
-
-
N1',N6'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide
-
-
N1',N6'-bis(2-(naphthalen-2-yloxy)acetyl)adipohydrazide
-
-
N1-(6,7-dimethoxyquinazolin-4-yl)benzene-1,4-diamine
14% inhibition at 2 mM
N1-(6,7-dimethoxyquinazolin-4-yl)cyclohexane-1,2-diamine
-
N1-(6-nitroquinazolin-4-yl)benzene-1,2-diamine
-
streptomycin
0.5 mg/ml, 74% reduction in activity
tert-butyl (2S,4S)-2-([4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl]carbamoyl)-4-hydroxypyrrolidine-1-carboxylate
-
UDP-N-acetyl-D-glucosamine
-
slight product inhibition in reverse reaction
UMP
-
inhibits catabolic reaction
ZINC70672706
interaction analysis
-
ZINC85867098
interaction analysis
-
ZINC95098775
interaction analysis
-
ZINC95098837
interaction analysis
-
ZINC95098867
interaction analysis
-
[4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl](3-hydroxyphenyl)methanone
7% inhibition at 0.05 mM
1-[(2S,3S,4R,5S)-3,4-dihydroxy-5-(hydroxymethyl)tetrahydrofuran-2-yl]dihydropyrimidine-2,4(1H,3H)-dione
-
-
1-[(2S,3S,4R,5S)-3,4-dihydroxy-5-(hydroxymethyl)tetrahydrofuran-2-yl]dihydropyrimidine-2,4(1H,3H)-dione
-
-
5-Hydroxyuridine
-
-
diphosphate
0.5 mM, 56% reduction in activity
diphosphate
-
slight inhibition above 8 mM
diphosphate
-
above 75 mM
EDTA
5 mM, 11% residual activity
EDTA
-
not reversible by addition of Mg2+
fluoride
-
inhibits Mg2+ but not Mn2+ activated enzyme
fluoride
-
slight inhibition
Mercuric chloride
-
-
Mercuric chloride
-
complete inactivation with 0.5 mM at 30°C, 45 min, reversible by addition of 1 mM dithiothreitol
N-[4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl]benzamide
44% inhibition at 2 mM
N-[4-[(6,7-dimethoxyquinazolin-4-yl)amino]phenyl]benzamide
44% inhibition; 44% inhibition at 0.05 mM
N-[4-[(7-hydroxy-6-methoxyquinazolin-4-yl)amino]phenyl]benzamide
36% inhibition at 2 mM
N-[4-[(7-hydroxy-6-methoxyquinazolin-4-yl)amino]phenyl]benzamide
36% inhibition; 36% inhibition at 0.05 mM
p-chloromercuribenzoate
-
completely reversible with cysteine
p-chloromercuribenzoate
-
-
pseudouridine
-
-
uridine
-
-
uridine
-
competitive with diphosphate, noncompetitive with UDP-N-acetyl-D-glucosamine, activity could be restored by dialysis
additional information
docking analysis of inhibitors, overview
-
additional information
-
docking analysis of inhibitors, overview
-
additional information
no inhibition with terreic acid, isolated from Aspergillus terreus, the compound inhibits the acetyltransferase activity of Escherichia coli GlmU but not the uridinyltransferase activity
-
additional information
terreic acid inhibits the glucosamine-1-phosphate-acetyltransferase activity of the bifunctional enzyme. Mode of inhibition studies reveal that terreic acid is competitive with AcCoA and uncompetitive with GlcN-1-phosphate. It also exhibits concentration-dependent killing of Escherichia coli strain ATCC 25922 and inhibits the growth of biofilms generated by Escherichia coli. GlmU acetyltransferase is a molecular target of terreic acid, resulting in its antibacterial activity. Terreic acid is isolated from Aspergillus terreus strain MRCJ-356. Molecular modeling
-
additional information
-
N-acetylglucosamine derivative inhibitors design and synthesis, inhibitor docking studies and simulation, RMS and binding energies, overview
-
additional information
N-acetylglucosamine derivative inhibitors design and synthesis, inhibitor docking studies and simulation, RMS and binding energies, overview
-
additional information
-
displacement of MgB 2+ from its usual catalytically competent position, as noted in the crystal structure of RNA polymerase in an inactive state, is considered to be a key factor inhibiting the reaction. The entire metal-substrate complex renders the enzyme catalytically inactive
-
additional information
no inhibition by 6624116, 5655606, 5810599, and 6012954
-
additional information
design of bisubstrate and transition-state based inhibitors of GlmU uridyltransferase, the potential inhibitors against GlmU are initially prepared leading to the discovery of active minoquinazoline-based compounds with inhibitory potential against the uridyltransferase activity, compound synthesis, overview. No inhibition by 10, 11, 15, 16, 17, 32, and 34
-
additional information
dicumarol is unable to inhibit the N-acetylglucosamine-1-phosphate uridyltransferase activity of GlmU
-
additional information
inhibitory potential of 4-aminoquinazolines as Mycobacterium tuberculosis N-acetylglucosamine-1-phosphate uridyltransferase (GlmUMTB) inhibitors, overview. Molecular docking using the crystal structure of GlmUMTB (PDB ID 3ST8), with bound substrates, N-acetylglucosamine-1-phosphate (NAcGlc-1-P) and uridine diphosphate-N-cetylglucosamine (UDP-GlcNAc). Analysis of inhibition of Mycobacterium tuberculosis wild-type strain H37Rv and of multiresistant strain MDR-MTB, antimycobacterial activity, MIC values for both strains; not inhibited by isoniazid
-
additional information
-
TbUAP inhibitor by high-throughput screening, and structure-activity relationships, overview. No inhibition by 3
-
additional information
-
for development of potent and selective inhibitors of the uridyltransferase activity of Xanthomonas oryzae pv. oryzae GlmU, three types of target compounds are optimized and synthesized based on the Xo-GlmU structure, docking stud, and biological activity evaluation, overview
-
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0.00996
(Z)-4-(4-(benzyloxy)benzylidene)-2-(naphthalen-1-yl)oxazol-5(4H)-one
Mycobacterium tuberculosis
pH 7.4, 37°C
0.0087
2-2-[(6-nitroquinazolin-4-yl)amino]ethoxy)-ethan-1-ol
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0087
2-[2-[(6-nitroquinazolin-4-yl)amino]ethoxy]-ethan-1-ol
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.037
3-[2-(1,3-benzodioxol-5-yl)-2-oxoethyl]-4-bromo-3-hydroxy-5-methyl-1,3-dihydro-2H-indol-2-one
Trypanosoma brucei brucei
pH not specified in the publication, temperature not specified in the publication
0.037
3-[2H-(1,3-benzodioxol-5-yl)-2-oxoethyl]-4-bromo-3-hydroxy-5-methyl-1,3-dihydro-2H-indol-2-one
Trypanosoma brucei
-
pH 7.5, temperature not specified in the publication
0.2
4-(5-[(6-nitroquinazolin-4-yl)amino]-1,3,4-thiadiazol-2-yl)phenol
Mycobacterium tuberculosis
above, pH and temperature not specified in the publication
0.042
4-(6-nitroquinazolin-4-ylamino)benzoic acid
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.018
4-chloro-N-(3-methoxypropyl)-N-[1-(2-phenylethyl)piperidin-3-yl]benzamide
Haemophilus influenzae
-
0.1
4-chloro-N-[1-[2-(2-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide
Haemophilus influenzae
value above
0.1
4-chloro-N-[1-[2-(3-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide
Haemophilus influenzae
value above
0.089
4-chloro-N-[1-[2-(4-fluorophenyl)ethyl]piperidin-3-yl]-N-(3-methoxypropyl)benzamide
Haemophilus influenzae
-
0.02
4-fluoro-N-(3-methoxypropyl)-N-[1-(2-phenylethyl)piperidin-3-yl]benzamide
Haemophilus influenzae
-
0.2
4-methyl-7-[(6-nitroquinazolin-4-yl)amino]-2H-1-benzopyran-2-one
0.026
4-[(6-nitroquinazolin-4-yl)amino]-N-(pyrimidin-2-yl)benzene-1-sulfonamide
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.2
4-[5-[(6-nitroquinazolin-4-yl)amino]-1,3,4-thiadiazol-2-yl]phenol
Mycobacterium tuberculosis
IC50 above 0.2 mM, pH and temperature not specified in the publication
0.016
6-nitro-N-(1,3-thiazol-2-yl)quinazolin-4-amine
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.021
6-nitro-N-(3,4,5-trimethoxyphenyl)quinazolin-4-amine
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.2
6-nitro-N-(5-phenyl-1,3,4-thiadiazol-2-yl)quinazolin-4-amine
0.023
6-nitro-N-(pyridin-2-ylmethyl)quinazolin-4-amine
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.2
6-nitro-N-[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]quinazolin-4-amine
0.021
6-nitro-N-[5-(trifluoromethyl)-1,3,4-thiadiazol-2-yl]quinazolin-4-amine
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.00081
luteolin
Xanthomonas oryzae pv. oryzae
pH 7.5, 37°C
0.023
N'-[(4-chloro-3,5-dimethylphenoxy)acetyl]-2,4-dihydroxybenzohydrazide
Xanthomonas oryzae pv. oryzae
pH 7.5, 37°C
0.014
N'1,N'6-bis[2-(naphthalen-2-yloxy)acetyl]hexanedihydrazide
Xanthomonas oryzae pv. oryzae
pH 7.5, 37°C
0.0029
N-(1-benzylpiperidin-4-yl)-6-nitroquinazolin-4-amine
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.052
N-(2,4-dimethylphenyl)-6-nitroquinazolin-4-amine
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.049
N-(3,5-dimethoxyphenyl)-2,3-dihydro-4H-1,4-benzothiazine-4-carboxamide
Trypanosoma brucei
-
pH 7.5, temperature not specified in the publication
0.194
N-(3-methylpiperazin-1-yl)-6-nitroquinazolin-4-amine
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.074
N-(4-((6,7-dimethoxyquinazolin-4-yl)amino)phenyl)-3-hydroxybenzamide
Mycobacterium tuberculosis
pH 7.6, 37°C
0.028
N-(4-[(6-nitroquinazolin-4-yl)amino]benzene-1-sulfonyl)acetamide
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.2
N-(5-methyl-1,3,4-thiadiazol-2-yl)-6-nitroquinazolin-4-amine
0.0064
N-carbamimidoyl-4-[(6-nitroquinazolin-4-yl)-amino]benzene-1-sulfonamide
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.141
N-cyclohexyl-6-nitroquinazolin-4-amine
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.121
N-cyclopropyl-6-nitroquinazolin-4-amine
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.028
N-[4-[(6-nitroquinazolin-4-yl)amino]benzene-1-sulfonyl]acetamide
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.2
N-[5-(2-chlorophenyl)-1,3,4-thiadiazol-2-yl]-6-nitroquinazolin-4-amine
0.0108
N1',N3'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37°C
0.0184
N1',N3'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37°C
0.0134
N1',N3'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)isophthalohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37°C
0.0138
N1',N3'-bis(2-(naphthalen-2-yloxy)acetyl) isophthalohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37°C
0.0154
N1',N4'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37°C
0.0194
N1',N4'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37°C
0.0112
N1',N4'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)succinohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37°C
0.0171
N1',N4'-bis(2-(naphthalen-2-yloxy)acetyl) succinohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37°C
0.0233
N1',N6'-bis(2-(1-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37°C
0.022
N1',N6'-bis(2-(3-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37°C
0.0125
N1',N6'-bis(2-(6-bromonaphthalen naphthalen-2-yloxy)acetyl)adipohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37°C
0.0332
N1',N6'-bis(2-(naphthalen-2-yloxy)acetyl)adipohydrazide
Xanthomonas oryzae pv. oryzae
-
pH 7.5, 37°C
0.0104
N1-(6-nitroquinazolin-4-yl)benzene-1,2-diamine
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0000063
rifampicin
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.2
4-methyl-7-[(6-nitroquinazolin-4-yl)amino]-2H-1-benzopyran-2-one
Mycobacterium tuberculosis
above, pH and temperature not specified in the publication
0.2
4-methyl-7-[(6-nitroquinazolin-4-yl)amino]-2H-1-benzopyran-2-one
Mycobacterium tuberculosis
IC50 above 0.2 mM, pH and temperature not specified in the publication
0.2
6-nitro-N-(5-phenyl-1,3,4-thiadiazol-2-yl)quinazolin-4-amine
Mycobacterium tuberculosis
above, pH and temperature not specified in the publication
0.2
6-nitro-N-(5-phenyl-1,3,4-thiadiazol-2-yl)quinazolin-4-amine
Mycobacterium tuberculosis
IC50 above 0.2 mM, pH and temperature not specified in the publication
0.2
6-nitro-N-[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]quinazolin-4-amine
Mycobacterium tuberculosis
above, pH and temperature not specified in the publication
0.2
6-nitro-N-[5-(4-methylphenyl)-1,3,4-thiadiazol-2-yl]quinazolin-4-amine
Mycobacterium tuberculosis
IC50 above 0.2 mM, pH and temperature not specified in the publication
0.2
N-(5-methyl-1,3,4-thiadiazol-2-yl)-6-nitroquinazolin-4-amine
Mycobacterium tuberculosis
above, pH and temperature not specified in the publication
0.2
N-(5-methyl-1,3,4-thiadiazol-2-yl)-6-nitroquinazolin-4-amine
Mycobacterium tuberculosis
IC50 above 0.2 mM, pH and temperature not specified in the publication
0.2
N-[5-(2-chlorophenyl)-1,3,4-thiadiazol-2-yl]-6-nitroquinazolin-4-amine
Mycobacterium tuberculosis
above, pH and temperature not specified in the publication
0.2
N-[5-(2-chlorophenyl)-1,3,4-thiadiazol-2-yl]-6-nitroquinazolin-4-amine
Mycobacterium tuberculosis
IC50 above 0.2 mM, pH and temperature not specified in the publication
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evolution
although Entamoeba histolytica UAP exhibits the same three-domain global architecture as other UAPs, it appears to lack three alpha-helices at the N-terminus and contains two amino acids in the allosteric pocket that make it appear more like the enzyme from the human host than that from the other parasite Trypanosoma brucei
evolution
GlmU belongs to the large family of sugar nucleotidyl transferases, which can be classified into group-I, which employs the two-metal mechanism-B as in GlmU, and group-II that employs a variant one metal mechanism-B, wherein the role of Mg2+ A is substituted by a conserved lysine. Eukaryotic sugar nucleotidyl transferases appear confined to group-II, structure-based sequence comparisons of sugar nucleotidyl transferases
evolution
organization andexpression of the mmy gene in Drosophila species, overview
evolution
-
the GlmU proteins encoded by Yersinia pestis and Yersinia pseudotuberculosis are identical in amino acid sequence
evolution
-
the N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme exclusive to prokaryotes, that belongs to the family of sugar nucleotidyltransferases (SNTs)
evolution
UAP isozymes are encoded by two different genes, LmUAP1 and LmUAP2
evolution
comparison of the activities of the ST0452 protein to those of similar enzymes from bacteria show that both the apparent Km and kcat values of the ST0452 GlcNAc-1-P UTase activity are smaller than those of Escherichia coli GlmU (EcGlmU) enzymes indicating that the archaeal ST0452 protein can accept a low concentration of substrate but that its turnover rate is lower than that of the EcGlmU enzyme
evolution
-
comparison of the activities of the ST0452 protein to those of similar enzymes from bacteria show that both the apparent Km and kcat values of the ST0452 GlcNAc-1-P UTase activity are smaller than those of Escherichia coli GlmU (EcGlmU) enzymes indicating that the archaeal ST0452 protein can accept a low concentration of substrate but that its turnover rate is lower than that of the EcGlmU enzyme
-
evolution
-
the GlmU proteins encoded by Yersinia pestis and Yersinia pseudotuberculosis are identical in amino acid sequence
-
malfunction
GlmUMtb depletion perturbs cell wall structure and affects the bacterial survival in normoxia, overview
malfunction
independently-derived mmy mutants exhibit a variety of highly penetrant phenotypes, ranging from cuticle defects associated with a failure to synthesize chitin to cuticle defects associated with well-characterized Dpp-dependent closure abnormalities (dorsal closure and head involution). In particular, the mmy-associated cuticle defects are identical to those resulting from loss-of-function mutations in raw and anterior-open
malfunction
KT282116, KT282117
knockdown of LdUAP1 reduces chitin contents in whole larvae and integument samples, thins tracheal taenidia, impairs larval-larval molt, larval-pupal ecdysis and adult emergence. Combined knockdown of LdUAP1 and LdUAP2 causes an additive negative effect. Phenotypes, overview
malfunction
KT282116, KT282117
silencing of LdUAP2 significantly reduces foliage consumption, decreases chitin content in midgut samples, damages PM, and retards larval growth. The resulting larvae have lighter fresh weights, smaller body sizes and depleted fat body. As a result, the development is arrested. Combined knockdown of LdUAP1 and LdUAP2 causes an additive negative effect. Phenotypes, overview
malfunction
the inhibition of this enzyme results in the fungal cell death
malfunction
the lesion mimic spl29 mutant exhibits spotted leaves and rapid leaf senescence from the seedling stage throughout the rest of its life cycle, leaf phenotype of wild-type and spl29 mutant plants, overview. The phenotype of spl29 is controlled by a single recessive nuclear gene, functional complementation with LOC_Os08g10600 in the spl29 mutant. Irreversible degradation of chloroplasts occurs in early senescent leaves of spl29 mutants. The early senescence phenotype involves upregulated expression levels of senescence-associated transcription factors and senescence-associated genes, and downregulated expression levels of photosynthesis-related genes, overview. Reactive oxygen species and malondialdehyde, as well as abscisic acid and jasmonic acid accumulate in the spl29 mutant accompanied by increased superoxide dismutase activity and normal catalase activity
malfunction
the naturally occuring UAP1 A229T mutation is potentially pathogenic. The A229T mutation induces structural changes, leading to reduced thermal stability and activity of the mutant compared to wild-type
malfunction
-
GlmUMtb depletion perturbs cell wall structure and affects the bacterial survival in normoxia, overview
-
malfunction
-
GlmUMtb depletion perturbs cell wall structure and affects the bacterial survival in normoxia, overview
-
malfunction
-
the lesion mimic spl29 mutant exhibits spotted leaves and rapid leaf senescence from the seedling stage throughout the rest of its life cycle, leaf phenotype of wild-type and spl29 mutant plants, overview. The phenotype of spl29 is controlled by a single recessive nuclear gene, functional complementation with LOC_Os08g10600 in the spl29 mutant. Irreversible degradation of chloroplasts occurs in early senescent leaves of spl29 mutants. The early senescence phenotype involves upregulated expression levels of senescence-associated transcription factors and senescence-associated genes, and downregulated expression levels of photosynthesis-related genes, overview. Reactive oxygen species and malondialdehyde, as well as abscisic acid and jasmonic acid accumulate in the spl29 mutant accompanied by increased superoxide dismutase activity and normal catalase activity
-
metabolism
N-acetylglucosamine-1-phosphate uridyltransferase is a bifunctional enzyme that catalyzes both acetyltransfer and uridyltransfer reactions in the prokaryotic UDP-GlcNAc biosynthesis pathway
metabolism
the enzymeis involved in the UDP-N-acetylglucosamine synthesis pathway, overview
metabolism
the first committed step in the biosynthesis of peptidoglycan involves the formation of uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) from uridine triphosphate (UTP) and GlcNAc-1-phosphate. This reactionis catalysed by N-acetylglucosamine-1-phosphate uridyltransferase (GlmU), a bifunctional enzyme with two independent active sites that possess acetyltransferase and uridyltransferase activities
metabolism
the mmy-encoded N-acetylglucosamine pyrophosphorylase impacts multiple Drosophila developmental events via the action of several different downstream transferases, some of which modify proteins and lipids with GlcNAc
metabolism
uridine diphosphate N-acetylglucosamine pyrophosphorylase catalyzes the final step in the synthesis of UDP-GlcNAc, which is involved in cell-wall biogenesis in plants and fungi and in protein glycosylation
metabolism
the enzyme is involved in biosyntheis of UDP-N-acetylglucosamine
metabolism
the bifunctional enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan
metabolism
-
the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
metabolism
pathway and metabolism of UDP-N-acetylglucosamine in prokaryotes and eukaryotes, overview
metabolism
-
the enzyme is involved in biosyntheis of UDP-N-acetylglucosamine
-
metabolism
-
the bifunctional enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan
-
metabolism
-
the enzymeis involved in the UDP-N-acetylglucosamine synthesis pathway, overview
-
metabolism
-
the first committed step in the biosynthesis of peptidoglycan involves the formation of uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) from uridine triphosphate (UTP) and GlcNAc-1-phosphate. This reactionis catalysed by N-acetylglucosamine-1-phosphate uridyltransferase (GlmU), a bifunctional enzyme with two independent active sites that possess acetyltransferase and uridyltransferase activities
-
metabolism
-
the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
-
metabolism
-
pathway and metabolism of UDP-N-acetylglucosamine in prokaryotes and eukaryotes, overview
-
physiological function
down-regulation of transcripts by RNA interference prevents larval growth or results in pupal paralysis, depending on time of injection of double-stranded RNAs. Down-regulation of transcripts at the mature adult stage results in cessation of oviposition in females, as well as fat body depletion and eventual death in both sexes
physiological function
down-regulation of transcripts by RNA interference results for isoform UAP1 in specific arrest at the larval-larval, larval-pupal or pupal-adult molts, depending on time of injection of double-stranded RNAs, loss of structural integrity and chitin staining and loss of peritrophic matrix-associated chitin. Down-regulation of transcripts at the mature adult stage results in cessation of oviposition in females, as well as fat body depletion and eventual death in both sexes
physiological function
because the multifunctional ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
physiological function
the enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms
physiological function
injection of early second- and fifth-instar nymphs (1-day-old) or middle second- and fifth-instar nymphs (3- to 4-day-old) with UAP2 RNAi does not interfere with normal development and molting of insects
physiological function
injection of early second- and fifth-instar nymphs (1-day-old) with UAP1 RNAi results in 100% mortality 2 days after the injection. Injection of middle second- and fifth-instar nymphs (3- to 4-day-old) with UAP1 RNAi results in 100% mortality during their next molting process
physiological function
KT282116, KT282117
knockdown of UAP1 reduces chitin contents in whole larvae and integument samples, thinned tracheal taenidia, impairs larval-larval molt, larval-pupal ecdysis and adult emergence. Combined knockdown of UAP1 and UAP2 causes an additive negative effect
physiological function
KT282116, KT282117
silencing of LdUAP2 significantly reduces foliage consumption, decreases chitin content in midgut samples, damages peritrophic matrix, and retards larval growth
physiological function
spl29 mutants display early leaf senescence, chloroplast degradation and both upregulation of senescence transcription factors and senescence-associated genes, and downregulation of photosynthesis-related genes. Defence responses are induced in the spl29 mutant. Reactive oxygen species, including O2 and H2O2, accumulate in spl29 plants, there is also increased malondialdehyde content. The plant hormones jasmonic acid and abscisic acid also accumulate in spl29 plants
physiological function
the mmy gene product isoform RA is an orthologue of the yeast N-acetylglucosamine diphosphorylase QRI1. In Drosophila melanogaster, mmy mutants exhibit a variety of highly penetrant phenotypes, ranging from cuticle defects associated with a failure to synthesize chitin to cuticle defects associated with well-characterized decapentaplegic-dependent closure abnormalities. UDP-N-acetylglucosamine diphosphorylase activity is required to spatially limit decapentaplegic, the Drosophila melanogaster BMP homolog, activity in a JNK/AP-1-independent fashion
physiological function
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme involved in bacterial cell wall synthesis and is exclusive to prokaryotes
physiological function
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme, its N- and C-terminal domains catalyze uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively. Final product of GlmU catalyzed reaction
physiological function
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyze uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively. Final product of GlmU catalyzed reaction, uridine-diphospho-N-acetylglucosamine (UDP-GlcNAc), acts as sugar donor providing GlcNAc residues in the synthesis of peptidoglycan and a disaccharide linker (D-N-GlcNAc-1-rhamnose), the key structural components of Mycobacterium tuberculosis cell wall
physiological function
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is exclusive to prokaryotes and a bifunctional enzyme that synthesizes UDP-GlcNAc, an important component of the cell wall of many microorganisms
physiological function
SPL29 or UAP1 is probably involved in regulating leaf senescence and defence responses in rice. Leaf senescence is a complex process controlled by a large number of different genes
physiological function
the acetyl- and uridyltransferase activities of GlmUMtb are independently essential for bacterial survival in vitro, and GlmUMtb is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. The administration of Oxa33, a novel oxazolidine derivative that specifically inhibits GlmUMtb, to infected mice results in significant decrease in the bacillary load. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively
physiological function
-
the bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase enzyme GlmU is an essential gene in Yersinia
physiological function
-
the enzyme binds N-acetylglucosamine-1-phosphate and UTP, and catalyzes an uridyltransfer reaction to synthesize UDP-GlcNAc, an important precursor for cell-wall biosynthesis
physiological function
-
the enzyme catalyzes the final reaction in the biosynthesis of UDP-GlcNAc, an essential metabolite in many organisms including Trypanosoma brucei,
physiological function
the enzyme functions in the formation of extracellular matrix by producing N-acetylglucosamine (GlcNAc) residues needed for chitin biosynthesis and protein glycosylation
physiological function
KT282116, KT282117
the enzyme is involved in the biosynthesis of chitin, an essential component of the epidermal cuticle and midgut peritrophic matrix in insects
physiological function
the enzyme is one of the pathogen proteins that bind to human interleukin-8, IL-8. The binding interaction of mycobacterial proteins AtsG, GlmU and SahH with human IL-8 may indicate that these proteins participate in the modulation of the early events of infection with tubercle bacilli and could affect pathogen attachment to target cells. Interleukin-8 belongs to the family of CXC chemokines and functions as a chemoattractant and activator of different subsets of leukocytes
physiological function
the JNK/AP-1 signaling cascade transcriptionally activates BMP signaling in leading edge epidermal cells, while the mummy (mmy) gene product is required for dorsal closure, and functions as a BMP signaling antagonist. The evolutionarily conserved JNK/AP-1 (Jun N-terminal kinase/activator protein 1) and BMP (bone morphogenetic protein) signaling cascades are deployed hierarchically to regulate dorsal closure in the fruit fly Drosophila melanogaster. The mmy gene product is a type of epidermal BMP regulator that transforms a BMP ligand from a long to a short range signal. Gene mmy codes for the single UDP-N-acetylglucosamine pyrophosphorylase in Drosophila, and its requirement for attenuating epidermal BMP signaling during dorsal closure points to another role for glycosylation in defining a highly restricted BMP activity field in the fly. In addition to being the building block of chitin, UDP-GlcNAc is an essential precursor for the synthesis of heparin and chondroitin sulfate proteoglycans, the former having been shown to play an essential role in modulating the effects of Dpp/BMP, Wingless (Wg)/WNT, and Hedgehog (Hh) morphogen signaling in Drosophila and other eukaryotes, usually as a facilitator of long-range signaling. Crucial role for Mmy in regulating embryonic Dpp signaling. Mmy modulation of Dpp signaling is Dpp-dependent and AP-1-independent
physiological function
the product of the GlmU catalyzed reactions, UDP-N-acetylglucosamine, is a significant precursor for the peptidoglycan and LPS biosynthesis in Gram-positive and Gram-negative bacteria, respectively
physiological function
UDP-N-acetylglucosamine pyrophosphorylase (UNAcP) is a key enzyme to construct the fungal cell wall
physiological function
the ST0452 protein, a thermostable protein isolated from the thermophilic archaeon Sulfolobus tokodaii, is a bifunctional protein exhibiting sugar-1-phosphate nucleotidylyltransferase (sugar-1-PNTase) and amino-sugar-1-phosphate acetyltransferase activities. ST0452 protein exhibits increased activity following single amino acid substitutions of Ala
physiological function
enzyme ST0452 is multifunctional
physiological function
the bifunctional enzyme is found exclusively in bacteria and catalyzes the development of uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc), an essential intermediate in peptidoglycan biosynthesis in Mycobacterium tuberculosis (Mtb)
physiological function
the enzyme is essential for chitin synthesis
physiological function
UDP-N-acetylglucosamine diphosphorylase of Bombyx mori (BmUAP) is an essential enzyme for chitin synthesis in insects. The higher levels of gene expression in integument infer that BmUAP has a significant role in cuticle formation and molting
physiological function
-
because the multifunctional ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
-
physiological function
-
the enzyme is involved in biosynthesis of UDP-N-acetyl-alpha-D-glucosamine, an activated and essential form of N-acetyl-alpha-D-glucosamine that is an important component in the polysaccharide structure of most organisms
-
physiological function
-
enzyme ST0452 is multifunctional
-
physiological function
-
the ST0452 protein, a thermostable protein isolated from the thermophilic archaeon Sulfolobus tokodaii, is a bifunctional protein exhibiting sugar-1-phosphate nucleotidylyltransferase (sugar-1-PNTase) and amino-sugar-1-phosphate acetyltransferase activities. ST0452 protein exhibits increased activity following single amino acid substitutions of Ala
-
physiological function
-
enzyme ST0452 is multifunctional
-
physiological function
-
enzyme ST0452 is multifunctional
-
physiological function
-
the enzyme is one of the pathogen proteins that bind to human interleukin-8, IL-8. The binding interaction of mycobacterial proteins AtsG, GlmU and SahH with human IL-8 may indicate that these proteins participate in the modulation of the early events of infection with tubercle bacilli and could affect pathogen attachment to target cells. Interleukin-8 belongs to the family of CXC chemokines and functions as a chemoattractant and activator of different subsets of leukocytes
-
physiological function
-
the acetyl- and uridyltransferase activities of GlmUMtb are independently essential for bacterial survival in vitro, and GlmUMtb is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. The administration of Oxa33, a novel oxazolidine derivative that specifically inhibits GlmUMtb, to infected mice results in significant decrease in the bacillary load. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively
-
physiological function
-
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyze uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively. Final product of GlmU catalyzed reaction, uridine-diphospho-N-acetylglucosamine (UDP-GlcNAc), acts as sugar donor providing GlcNAc residues in the synthesis of peptidoglycan and a disaccharide linker (D-N-GlcNAc-1-rhamnose), the key structural components of Mycobacterium tuberculosis cell wall
-
physiological function
-
the bifunctional enzyme is found exclusively in bacteria and catalyzes the development of uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc), an essential intermediate in peptidoglycan biosynthesis in Mycobacterium tuberculosis (Mtb)
-
physiological function
-
the product of the GlmU catalyzed reactions, UDP-N-acetylglucosamine, is a significant precursor for the peptidoglycan and LPS biosynthesis in Gram-positive and Gram-negative bacteria, respectively
-
physiological function
-
the enzyme is one of the pathogen proteins that bind to human interleukin-8, IL-8. The binding interaction of mycobacterial proteins AtsG, GlmU and SahH with human IL-8 may indicate that these proteins participate in the modulation of the early events of infection with tubercle bacilli and could affect pathogen attachment to target cells. Interleukin-8 belongs to the family of CXC chemokines and functions as a chemoattractant and activator of different subsets of leukocytes
-
physiological function
-
the acetyl- and uridyltransferase activities of GlmUMtb are independently essential for bacterial survival in vitro, and GlmUMtb is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. The administration of Oxa33, a novel oxazolidine derivative that specifically inhibits GlmUMtb, to infected mice results in significant decrease in the bacillary load. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively
-
physiological function
-
the bifunctional enzyme is found exclusively in bacteria and catalyzes the development of uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc), an essential intermediate in peptidoglycan biosynthesis in Mycobacterium tuberculosis (Mtb)
-
physiological function
-
the bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase enzyme GlmU is an essential gene in Yersinia
-
physiological function
-
spl29 mutants display early leaf senescence, chloroplast degradation and both upregulation of senescence transcription factors and senescence-associated genes, and downregulation of photosynthesis-related genes. Defence responses are induced in the spl29 mutant. Reactive oxygen species, including O2 and H2O2, accumulate in spl29 plants, there is also increased malondialdehyde content. The plant hormones jasmonic acid and abscisic acid also accumulate in spl29 plants
-
physiological function
-
SPL29 or UAP1 is probably involved in regulating leaf senescence and defence responses in rice. Leaf senescence is a complex process controlled by a large number of different genes
-
physiological function
-
enzyme ST0452 is multifunctional
-
additional information
GlmU forms a biological trimer, and two independent domains in each monomer catalyze two independent reactions in the protein. The enzyme uses a two-metal ion mechanism (mechanism-B). In contrast to well-established two-metal mechanism (mechanism-A) for enzymes acting on nucleic acids, mechanism-B is distinct in the way the two Mg2+ ions (Mg2+A and Mg2+B) are positioned and stabilized. Analysis of the catalytic mechanism for the uridyltransfer reaction in GlmU, role of metal ions in substrate binding, overview
additional information
GlmU from Mycobacterium tuberculosis possesses a unique 30-residue extension at the C-terminus
additional information
-
GlmU from Mycobacterium tuberculosis possesses a unique 30-residue extension at the C-terminus
additional information
the EhUAP binding pocket largely appears consistent with other UAPs and is likely to follow the common UAP mechanism
additional information
the EhUAP binding pocket largely appears consistent with other UAPs and is likely to follow the common UAP mechanism
additional information
the ST0452 protein contains only two Cys residues, it is unlikely that CysCys bonds contribute to its thermostability
additional information
-
the ST0452 protein contains only two Cys residues, it is unlikely that CysCys bonds contribute to its thermostability
additional information
the Tyr103-Asp105 segment is located at the floor of the uridyltransferase active pocket and is involved in interactions with UTP and GlcNAc-1-P substrates
additional information
Tyr at the 97th position of the ST0452 protein plays an important role in catalysis. Reaction scheme of the sugar-1-P UTase, overview
additional information
-
Tyr at the 97th position of the ST0452 protein plays an important role in catalysis. Reaction scheme of the sugar-1-P UTase, overview
additional information
analysis of the overall structure of wild-type ST0452 protein (PDB ID 2GGO), residue 97 (Asn) interacts with the O-5 atom of N-acetylglucosamine (GlcNAc) in the complex without metal ions. UTP forms hydrogen bond interactions with seven residues, i.e. the main chain atoms of the position 8 Ala, position 9 Gly, position 12 Glu, position 79 Gly, and position 98 Gly residues and the side chain atoms of the position 13 Arg and position 73 Gln residues. The position 13 Arg and position 73 Gln residues appear to form more stable interactions than the other residues, with the position 13 Arg residue forming two hydrogen bonds with the phosphoryl group at the gamma-site and the amide group of the position 73 Gln residue forming a salt bridge with the uracil nucleobase in UTP
additional information
-
analysis of the overall structure of wild-type ST0452 protein (PDB ID 2GGO), residue 97 (Asn) interacts with the O-5 atom of N-acetylglucosamine (GlcNAc) in the complex without metal ions. UTP forms hydrogen bond interactions with seven residues, i.e. the main chain atoms of the position 8 Ala, position 9 Gly, position 12 Glu, position 79 Gly, and position 98 Gly residues and the side chain atoms of the position 13 Arg and position 73 Gln residues. The position 13 Arg and position 73 Gln residues appear to form more stable interactions than the other residues, with the position 13 Arg residue forming two hydrogen bonds with the phosphoryl group at the gamma-site and the amide group of the position 73 Gln residue forming a salt bridge with the uracil nucleobase in UTP
additional information
enzyme structure modeling and structure comparisons, detailed overview. Conformational changes occur in apo- and ligand-bound BmUAPs. Docking and molecular dynamics simulation studies of ligand-bound complexes of BmUAP, determination of binding mode of UTP, GlcNAc-1-P, and UDP-GlcNAc
additional information
-
enzyme structure modeling and structure comparisons, detailed overview. Conformational changes occur in apo- and ligand-bound BmUAPs. Docking and molecular dynamics simulation studies of ligand-bound complexes of BmUAP, determination of binding mode of UTP, GlcNAc-1-P, and UDP-GlcNAc
additional information
the human UAP1 gene encodes two different isoforms, named AGX1 and AGX2, with AGX1 being more abundant in testis and AGX2 in somatic tissues
additional information
-
the ST0452 protein contains only two Cys residues, it is unlikely that CysCys bonds contribute to its thermostability
-
additional information
-
analysis of the overall structure of wild-type ST0452 protein (PDB ID 2GGO), residue 97 (Asn) interacts with the O-5 atom of N-acetylglucosamine (GlcNAc) in the complex without metal ions. UTP forms hydrogen bond interactions with seven residues, i.e. the main chain atoms of the position 8 Ala, position 9 Gly, position 12 Glu, position 79 Gly, and position 98 Gly residues and the side chain atoms of the position 13 Arg and position 73 Gln residues. The position 13 Arg and position 73 Gln residues appear to form more stable interactions than the other residues, with the position 13 Arg residue forming two hydrogen bonds with the phosphoryl group at the gamma-site and the amide group of the position 73 Gln residue forming a salt bridge with the uracil nucleobase in UTP
-
additional information
-
Tyr at the 97th position of the ST0452 protein plays an important role in catalysis. Reaction scheme of the sugar-1-P UTase, overview
-
additional information
-
analysis of the overall structure of wild-type ST0452 protein (PDB ID 2GGO), residue 97 (Asn) interacts with the O-5 atom of N-acetylglucosamine (GlcNAc) in the complex without metal ions. UTP forms hydrogen bond interactions with seven residues, i.e. the main chain atoms of the position 8 Ala, position 9 Gly, position 12 Glu, position 79 Gly, and position 98 Gly residues and the side chain atoms of the position 13 Arg and position 73 Gln residues. The position 13 Arg and position 73 Gln residues appear to form more stable interactions than the other residues, with the position 13 Arg residue forming two hydrogen bonds with the phosphoryl group at the gamma-site and the amide group of the position 73 Gln residue forming a salt bridge with the uracil nucleobase in UTP
-
additional information
-
analysis of the overall structure of wild-type ST0452 protein (PDB ID 2GGO), residue 97 (Asn) interacts with the O-5 atom of N-acetylglucosamine (GlcNAc) in the complex without metal ions. UTP forms hydrogen bond interactions with seven residues, i.e. the main chain atoms of the position 8 Ala, position 9 Gly, position 12 Glu, position 79 Gly, and position 98 Gly residues and the side chain atoms of the position 13 Arg and position 73 Gln residues. The position 13 Arg and position 73 Gln residues appear to form more stable interactions than the other residues, with the position 13 Arg residue forming two hydrogen bonds with the phosphoryl group at the gamma-site and the amide group of the position 73 Gln residue forming a salt bridge with the uracil nucleobase in UTP
-
additional information
-
the ST0452 protein contains only two Cys residues, it is unlikely that CysCys bonds contribute to its thermostability
-
additional information
-
analysis of the overall structure of wild-type ST0452 protein (PDB ID 2GGO), residue 97 (Asn) interacts with the O-5 atom of N-acetylglucosamine (GlcNAc) in the complex without metal ions. UTP forms hydrogen bond interactions with seven residues, i.e. the main chain atoms of the position 8 Ala, position 9 Gly, position 12 Glu, position 79 Gly, and position 98 Gly residues and the side chain atoms of the position 13 Arg and position 73 Gln residues. The position 13 Arg and position 73 Gln residues appear to form more stable interactions than the other residues, with the position 13 Arg residue forming two hydrogen bonds with the phosphoryl group at the gamma-site and the amide group of the position 73 Gln residue forming a salt bridge with the uracil nucleobase in UTP
-
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K421A
the activity of the mutant is very low (less than 5%) in comparison to the wild type enzyme
D105A
site-directed mutagenesis, the mutant shows 50% reduced activity compared to the wild-type enzyme
DELTA1-130
-
deletion of N-terminus, very low activity
DELTA1-182
-
deletion of N-terminus, very low activity
DELTA1-227
-
deletion of N-terminus, very low activity
DELTA1-233
-
deletion of N-terminus, very low activity
DELTA1-250
-
deletion of N-terminus
DELTA1-26
-
deletion of N-terminus
DELTA1-78
-
deletion of N-terminus, very low activity
DELTA227-456
-
deletion of C-terminus
DELTA250-456
-
deletion of C-terminus, low activity
DELTA331-456
-
deletion of C-terminus, roughly 50% of activity
E154D
site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 80% reduced activity compared to the wild-type enzyme
E154K
site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 90% reduced activity compared to the wild-type enzyme
E154L
site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 70% reduced activity compared to the wild-type enzyme
N169A
site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 50% reduced activity compared to the wild-type enzyme
N169D
site-directed mutagenesis in the GlcNAc-binding region, the mutant shows unaltered activity compared to the wild-type enzyme
N169Q
site-directed mutagenesis in the GlcNAc-binding region, the mutant shows unaltered activity compared to the wild-type enzyme
N169R
site-directed mutagenesis in the GlcNAc-binding region, the mutant shows 1.4fold increased activity compared to the wild-type enzyme. The N169R mutant caused a slightly secondary structure changes, thus facilitating GlcNAc-1-phosphate to enter the active pocket through the additional interaction with N-acetyl arm of GlcNAc moiety
Q76A
site-directed mutagenesis in the uridine-binding region, the mutant has a catalytic activity to convert CTP and GlcNAc-1P into unnatural sugar nucleotide CDP-GlcNAc which is distinct from the wild-type, altered nucleotide specificity compared to wild-type, overview
Q76E
site-directed mutagenesis in the uridine-binding region, the mutant has a catalytic activity to convert CTP and GlcNAc-1P into unnatural sugar nucleotide CDP-GlcNAc which is distinct from the wild-type, altered nucleotide specificity compared to wild-type, overview
Q76P
site-directed mutagenesis in the uridine-binding region, the mutant has a catalytic activity to convert CTP and GlcNAc-1P into unnatural sugar nucleotide CDP-GlcNAc which is distinct from the wild-type, altered nucleotide specificity compared to wild-type, overview
T82G
site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 65% reduced activity compared to the wild-type enzyme
T82Q
site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 80% reduced activity compared to the wild-type enzyme
T82S
site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 80% reduced activity compared to the wild-type enzyme
Y103F
site-directed mutagenesis of the residue located nearby the uridyltransferase active pocket,the mutant shows increased activity compared to the wild-type enzyme
Y103V
mutant protein shows a 30% decrease in activity compared to that of the wild-type enzyme
DELTA1-130
-
deletion of N-terminus, very low activity
-
DELTA1-182
-
deletion of N-terminus, very low activity
-
DELTA1-227
-
deletion of N-terminus, very low activity
-
DELTA1-26
-
deletion of N-terminus
-
DELTA1-78
-
deletion of N-terminus, very low activity
-
Y103V
-
mutant protein shows a 30% decrease in activity compared to that of the wild-type enzyme
-
G108A
dramatically reduced activity, significant increase in melting temperature
G210A
dramatically reduced activity, significant decrease in melting temperature
A229T
naturally occuring enzyme AGX1 mutation, and site-directed mutagenesis, the A229T mutation causes a reduction of protein thermal stability compared to wild-type AGX1, and AGX1A229T has lower activity in producing UDP-GlcNA. In diploid organisms, haploinsufficiency is a phenomenon in which a single copy of a functional gene is not sufficient to produce the normal/wild-type phenotype. The patient is only heterozygous for the UAP1 A229T missense mutation. The UAP1 gene is potentially haploinsufficient and LoF intolerant, and the heterozygous UAP1 A229T mutation is potentially pathogenic. The recombinant mutant enzyme shows a reduction of the melting temperature (Tm) by approximately 5.3°C compared to wild-type. The A229T mutation induces structural changes. The R228-E44 interaction is abolished in the AGX1A229T structure caused by the position shift of R228. The pushing effect is likely due to the bulkier side chain of threonine compared to that of alanine. Along with the conformational change of the N-terminal domain in the AGX1A229T structure, is M218 shifted by 0.8 A away from R169, weakening the Q112-R169-M218 interaction
F383A
the mutant can use GalNAzMe-1-phosphate as substrate
F383G
the mutant cannot use GalNAzMe-1-phosphate as substrate
G111A
-
very low activity
G222A
-
traces of activity in forward and reverse reaction with N-acetyl-D-glucosamine 1-phosphate and N-acetyl-D-galactosamine 1-phosphate
G224A
-
low activity in forward and reverse reaction with N-acetyl-D-glucosamine 1-phosphate and N-acetyl-D-galactosamine 1-phosphate
P220A
-
only slight changes in activity with N-acetyl-D-glucosamine 1-phosphate and N-acetyl-D-galactosamine 1-phosphate
R115A
-
slight changes in Km
Y227A
-
only slight changes in activity with N-acetyl-D-glucosamine 1-phosphate and N-acetyl-D-galactosamine 1-phosphate
H374A
site-directed mutagenesis, the acetyltransferase active site mutant shows 1.7% of acetyltransferase activity and 96.7% of uridinyltransferase activity compared to the wild-type
K464A
site-directed mutagenesis, the mutant still shows acetyltransferase activity, the mutant shows 105.6% acetyltransferase activity and 97.9% of uridinyltransferase activity compared to the wild-type
N239A
the activity of the mutant is very low (less than 10%) in comparison to the wild type enzyme
N397A
site-directed mutagenesis, the acetyltransferase active site mutant shows 5.2% of acetyltransferase activity and 113.6% of uridinyltransferase activity compared to the wild-type
S416A
site-directed mutagenesis, the acetyltransferase active site mutant shows 100.9% of acetyltransferase activity and 96.4% of uridinyltransferase activity compared to the wild-type
T418A
site-directed mutagenesis, the acetyltransferase activity of mutant is severely compromised as compared with GlmUMtb wild-type, the mutant shows 2.4% acetyltransferase activity and 100.4% of uridinyltransferase activity compared to the wild-type
T418E
site-directed mutagenesis, the acetyltransferase activity of the T418E mutant that mimics a phosphorylated Thr, is severely compromised as compared with GlmUMtb wild-type, the mutant shows 2.2% acetyltransferase activity and 109.2% of uridinyltransferase activity compared to the wild-type
T418S
site-directed mutagenesis, the acetyltransferase activity of the mutant is compromised as compared with GlmUMtb wild-type, the mutant shows 19% acetyltransferase activity and 108.8% of uridinyltransferase activity compared to the wild-type
W460A
site-directed mutagenesis, the mutant displays almost complete loss in acetyltransferase activity, the mutant shows 8.4% acetyltransferase activity and 99.8% of uridinyltransferase activity compared to the wild-type
W460A/K64A
site-directed mutagenesis, the mutant shows 7.8% acetyltransferase activity and 104.7% of uridinyltransferase activity compared to the wild-type
N239A
-
the activity of the mutant is very low (less than 10%) in comparison to the wild type enzyme
-
D99A
no GlcNAc-1-P UTase activity
H308A
site-directed mutagenesis
K23A
no GlcNAc-1-P UTase activity
K337A
site-directed mutagenesis
K340A
site-directed mutagenesis
N331A
site-directed mutagenesis
T80C
site-directed mutagenesis, the mutant shows slightly reduced GlcNAc-1-P UTase activity compared to wild-type
T80D
site-directed mutagenesis, the mutant shows increased Glc-1-P UTase activity and reduced GlcNAc-1-P UTase activity compared to wild-type
T80E
site-directed mutagenesis, the mutant shows no Glc-1-P UTase activity and highly reduced GlcNAc-1-P UTase activity
T80F
site-directed mutagenesis, the mutant shows no and Glc-1-P UTase and GlcNAc-1-P UTase activity
T80G
site-directed mutagenesis, the mutant shows increased GlcNAc-1-P and Glc-1-P UTase activity compared to wild-type
T80H
site-directed mutagenesis, the mutant shows increased Glc-1-P UTase activity and reduced GlcNAc-1-P UTase activity compared to wild-type
T80I
site-directed mutagenesis, the mutant shows no Glc-1-P UTase and GlcNAc-1-P UTase activity
T80K
site-directed mutagenesis, the mutant shows no Glc-1-P UTase activity and highly reduced GlcNAc-1-P UTase activity
T80M
site-directed mutagenesis, the mutant shows reduced GlcNAc-1-P UTase activity and no Glc-1-P UTase activity
T80N
site-directed mutagenesis, the mutant shows increased GlcNAc-1-P UTase activity compared to wild-type
T80P
site-directed mutagenesis, the mutant shows slightly reduced GlcNAc-1-P UTase activity compared to wild-type
T80Q
site-directed mutagenesis, the mutant shows increased GlcNAc-1-P and Glc-1-P UTase activity compared to wild-type
T80R
site-directed mutagenesis, the mutant shows no Glc-1-P UTase activity and highly reduced GlcNAc-1-P UTase activity
T80S
site-directed mutagenesis, the mutant shows the mutant shows increased GlcNAc-1-P UTase activity compared to wild-type
T80V
site-directed mutagenesis, the mutant shows slightly reduced GlcNAc-1-P UTase activity compared to wild-type
T80W
site-directed mutagenesis, the mutant shows no Glc-1-P UTase activity and highly reduced GlcNAc-1-P UTase activity
T80Y
site-directed mutagenesis, the mutant shows no Glc-1-P UTase activity and highly reduced GlcNAc-1-P UTase activity
Y311A
site-directed mutagenesis
Y97W
inactive mutant enzyme
E146A
-
exhibits slightly weaker UDP-N-acetylglucosamine diphosphorylase activity than wild-type enzyme
-
G9A
-
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions
-
K147A
-
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions
-
T80A
-
site-directed mutagenesis, the mutant shows increased GlcNAc-1-P and Glc-1-P UTase activity compared to wild-type
-
T80D
-
site-directed mutagenesis, the mutant shows increased Glc-1-P UTase activity and reduced GlcNAc-1-P UTase activity compared to wild-type
-
T80P
-
site-directed mutagenesis, the mutant shows slightly reduced GlcNAc-1-P UTase activity compared to wild-type
-
T80S
-
site-directed mutagenesis, the mutant shows the mutant shows increased GlcNAc-1-P UTase activity compared to wild-type
-
Y97F
-
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions
-
D99A
-
no GlcNAc-1-P UTase activity
-
E146A
-
no GlcNAc-1-P UTase activity
-
G9A/T80A
-
specific GlcNAc-1-P UTase activity of the mutant enzyme is 35fold lower compared to specific activity of the wild-type enzyme
-
K147A
-
GlcNAc-1-P UTase activity is 25% of the activity of wild-type ST0452 protein
-
T80A
-
site-directed mutagenesis, the mutant shows increased GlcNAc-1-P and Glc-1-P UTase activity compared to wild-type
-
T80D
-
site-directed mutagenesis, the mutant shows increased Glc-1-P UTase activity and reduced GlcNAc-1-P UTase activity compared to wild-type
-
T80P
-
site-directed mutagenesis, the mutant shows slightly reduced GlcNAc-1-P UTase activity compared to wild-type
-
T80S
-
site-directed mutagenesis, the mutant shows the mutant shows increased GlcNAc-1-P UTase activity compared to wild-type
-
T80S/Y97N
-
the mutant enzyme shows 6.5times-higher activity, compared to that of the wild-type ST0452 protein, revealing that these two substituted residues function cooperatively to increase N-acetylglucosamine-1-phosphate uridyltransferase activity
-
Y97A
-
1.82fold increase in GlcNAc-1-P UTase activity compared to that of the wild-type enzyme
-
Y97V
-
3.56fold increase in GlcNAc-1-P UTase activity compared to that of the wild-type enzyme
-
T80A
-
site-directed mutagenesis, the mutant shows increased GlcNAc-1-P and Glc-1-P UTase activity compared to wild-type
-
T80D
-
site-directed mutagenesis, the mutant shows increased Glc-1-P UTase activity and reduced GlcNAc-1-P UTase activity compared to wild-type
-
T80P
-
site-directed mutagenesis, the mutant shows slightly reduced GlcNAc-1-P UTase activity compared to wild-type
-
T80S
-
site-directed mutagenesis, the mutant shows the mutant shows increased GlcNAc-1-P UTase activity compared to wild-type
-
T80A
-
site-directed mutagenesis, the mutant shows increased GlcNAc-1-P and Glc-1-P UTase activity compared to wild-type
-
T80D
-
site-directed mutagenesis, the mutant shows increased Glc-1-P UTase activity and reduced GlcNAc-1-P UTase activity compared to wild-type
-
T80P
-
site-directed mutagenesis, the mutant shows slightly reduced GlcNAc-1-P UTase activity compared to wild-type
-
T80S
-
site-directed mutagenesis, the mutant shows the mutant shows increased GlcNAc-1-P UTase activity compared to wild-type
-
Y103A
mutant protein shows a 24% increase in activity compared to that of the wild-type enzyme
Y103A
activity is 25% higher than that of the wild-type enzyme
Y103N
mutant protein shows a 32% increase in activity compared to that of the wild-type enzyme
Y103N
activity is 30% higher than that of the wild-type enzyme
Y103N
activity is 30% lower than that of the wild-type enzyme
Y103A
-
mutant protein shows a 24% increase in activity compared to that of the wild-type enzyme
-
Y103A
-
activity is 25% higher than that of the wild-type enzyme
-
Y103N
-
mutant protein shows a 32% increase in activity compared to that of the wild-type enzyme
-
Y103N
-
activity is 30% higher than that of the wild-type enzyme
-
Y103N
-
activity is 30% lower than that of the wild-type enzyme
-
D208A
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions
D208A
exhibits slightly weaker UDP-N-acetylglucosamine diphosphorylase activity than wild-type enzyme
D208A
GlcNAc-1-P UTase activity is 10% of the activity of wild-type ST0452 protein
E146A
exhibits slightly weaker UDP-N-acetylglucosamine diphosphorylase activity than wild-type enzyme
E146A
no GlcNAc-1-P UTase activity
G9A
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions
G9A
GlcNAc-1-P UTase activity is less than 5%
G9A
site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type
G9A/K147A
specific GlcNAc-1-P UTase activity of the mutant enzyme is 71.8fold lower compared to specific activity of the wild-type enzyme
G9A/K147A
activity is 71.8fold lower than that of the wild-type enzyme
G9A/K147A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type enzyme
G9A/T80A
specific GlcNAc-1-P UTase activity of the mutant enzyme is 35fold lower compared to specific activity of the wild-type enzyme
G9A/T80A
activity is 35fold lower than that of the wild-type enzyme
G9A/T80A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type enzyme
G9A/Y97A
no activity
G9A/Y97A
inactive mutant enzyme
G9A/Y97A
site-directed mutagenesis, inactive mutant
G9A/Y97F
specific GlcNAc-1-P UTase activity of the mutant enzyme is 14.5fold lower compared to specific activity of the wild-type enzyme
G9A/Y97F
activity is 14.5fold lower than that of the wild-type enzyme
G9A/Y97F
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
K147A
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions
K147A
GlcNAc-1-P UTase activity is 25% of the activity of wild-type ST0452 protein
K147A
site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type
R13A
shows the same activity as wild-type protein
R13A
GlcNAc-1-P UTase activity is 10% of the activity of wild-type ST0452 protein
T80A
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions
T80A
GlcNAc-1-P UTase activity is 56% of the activity of wild-type ST0452 protein
T80A
site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type
T80A
site-directed mutagenesis, the mutant shows increased GlcNAc-1-P and Glc-1-P UTase activity compared to wild-type
T80A/K147A
specific GlcNAc-1-P UTase activity of the mutant enzyme is 11.09fold lower compared to specific activity of the wild-type enzyme
T80A/K147A
activity is 11.1fold lower than that of the wild-type enzyme
T80A/K147A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
T80A/Y97A
specific GlcNAc-1-P UTase activity of the mutant enzyme is 31.4fold lower compared to specific activity of the wild-type enzyme
T80A/Y97A
activity is 31.4fold lower than that of the wild-type enzyme
T80A/Y97A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type enzyme
T80A/Y97F
specific GlcNAc-1-P UTase activity of the mutant enzyme is 25.1fold lower compared to specific activity of the wild-type enzyme
T80A/Y97F
activity is 25.1fold lower than that of the wild-type enzyme
T80A/Y97F
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type enzyme
T80L
no GlcNAc-1-P UTase activity
T80L
site-directed mutagenesis, the mutant shows reduced GlcNAc-1-P UTase activity and no Glc-1-P UTase activity
T80S/Y97N
the mutant enzyme shows 6.5times-higher activity, compared to that of the wild-type ST0452 protein, revealing that these two substituted residues function cooperatively to increase N-acetylglucosamine-1-phosphate uridyltransferase activity
T80S/Y97N
site-directed mutagenesis, the mutant shows 6.5times higher activity with N-acetylglucosamine-1-phosphate compared to that of the wild-type ST0452 protein
Y97A
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions
Y97A
1.82fold increase in GlcNAc-1-P UTase activity compared to that of the wild-type enzyme
Y97A
GlcNAc-1-P UTase activity is 66% of the activity of wild-type ST0452 protein
Y97A
activity is 1.83fold higher than that of the wild-type enzyme
Y97A
site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type
Y97A/K147A
specific GlcNAc-1-P UTase activity of the mutant enzyme is 11.9fold lower compared to specific activity of the wild-type enzyme
Y97A/K147A
activity is 11.9fold lower than that of the wild-type enzyme
Y97A/K147A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
Y97C
activity is 1.4fold lower than that of the wild-type enzyme
Y97C
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
Y97D
activity is 1.3fold higher than that of the wild-type enzyme
Y97D
site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type
Y97E
activity is 2.1fold lower than that of the wild-type enzyme
Y97E
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
Y97F
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions
Y97F
GlcNAc-1-P UTase activity is similar to wild-type ST0452 protein
Y97F
activity is 1.2fold higher than that of the wild-type enzyme
Y97F
site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type
Y97F/K147A
specific GlcNAc-1-P UTaseactivity of the mutant enzyme is 5.7fold lower compared to specific activity of the wild-type enzyme
Y97F/K147A
activity is 5.4fold lower than that of the wild-type enzyme
Y97F/K147A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
Y97G
activity is 1.2fold higher than that of the wild-type enzyme
Y97G
site-directed mutagenesis, the mutant exhibits slightly increased GlcNAc-1-P UTase activity compared to wild-type
Y97H
activity is 2.9fold higher than that of the wild-type enzyme
Y97H
site-directed mutagenesis, the mutant exhibits highly increased GlcNAc-1-P UTase activity compared to wild-type
Y97I
activity is 1.2fold higher than that of the wild-type enzyme
Y97I
site-directed mutagenesis, the mutant exhibits slightly increased GlcNAc-1-P UTase activity compared to wild-type
Y97K
activity is 1.35fold higher than that of the wild-type enzyme
Y97K
site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type
Y97L
activity is 1.5fold higher than that of the wild-type enzyme
Y97L
site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type
Y97M
activity is 1.3fold higher than that of the wild-type enzyme
Y97M
site-directed mutagenesis, the mutant exhibits slightly increased GlcNAc-1-P UTase activity compared to wild-type
Y97N
4.45fold increase in GlcNAc-1-P UTase activity compared to that of the wild-type enzyme
Y97N
the mutant enzyme exhibits over 4 times higher N-acetylglucosamine-1-phosphate uridyltransferase activity, compared with that of the wild-type ST0452 protein. The three-dimensional structure of the Y97N protein is not changed by this substitution but the interactions with the substrate are slightly modified, which might cause the activity to increase. The crystal structure of the Y97N protein shows that positions 146 (Glu) and 80 (Thr) form interactions with GlcNAc, and an engineering strategy is applied to these residues to increase activity
Y97N
activity is 4.5fold higher than that of the wild-type enzyme
Y97N
site-directed mutagenesis, the mutant exhibits highly increased GlcNAc-1-P UTase activity compared to wild-type
Y97N
naturally occuring mutation, the Y97N mutant of the ST0452 protein, isolated from Sulfolobus tokodaii, exhibits over 4times higher N-acetylglucosamine-1-phosphate (GlcNAc-1-P) uridyltransferase (UTase, EC 2.7.7.23) activity, compared with that of the wild-type ST0452 protein, three-dimensional structure analysis of the Y97N protein. The overall structure is almost identical to that of the wild-type ST0452 protein (PDB ID 2GGO), with residue 97 (Asn) interacting with the O-5 atom of N-acetylglucosamine (GlcNAc) in the complex without metal ions
Y97P
activity is 1.5fold higher than that of the wild-type enzyme
Y97P
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
Y97Q
activity is 2.3fold higher than that of the wild-type enzyme
Y97Q
site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type
Y97R
inactive mutant enzyme
Y97R
site-directed mutagenesis, inactive mutant
Y97S
activity is 1.97fold higher than that of the wild-type enzyme
Y97S
site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type
Y97T
activity is 2.1fold higher than that of the wild-type enzyme
Y97T
site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type
Y97V
3.56fold increase in GlcNAc-1-P UTase activity compared to that of the wild-type enzyme
Y97V
activity is 3.6fold higher than that of the wild-type enzyme
Y97V
site-directed mutagenesis, the mutant exhibits highly increased GlcNAc-1-P UTase activity compared to wild-type
G9A
-
site-directed mutagenesis, the mutant exhibits increased GlcNAc-1-P UTase activity compared to wild-type
-
G9A
-
GlcNAc-1-P UTase activity is less than 5%
-
Y97F
-
activity is 1.2fold higher than that of the wild-type enzyme
-
Y97F
-
GlcNAc-1-P UTase activity is similar to wild-type ST0452 protein
-
Y97N
-
the mutant enzyme exhibits over 4 times higher N-acetylglucosamine-1-phosphate uridyltransferase activity, compared with that of the wild-type ST0452 protein. The three-dimensional structure of the Y97N protein is not changed by this substitution but the interactions with the substrate are slightly modified, which might cause the activity to increase. The crystal structure of the Y97N protein shows that positions 146 (Glu) and 80 (Thr) form interactions with GlcNAc, and an engineering strategy is applied to these residues to increase activity
-
Y97N
-
4.45fold increase in GlcNAc-1-P UTase activity compared to that of the wild-type enzyme
-
C307S
-
site-directed mutagenesis
C307S
-
site-directed mutagenesis
-
additional information
KT282116
knockdown of LdUAP1 or combined knockdown of LdUAP1 and LdUAP2
additional information
KT282117
knockdown of LdUAP1 or combined knockdown of LdUAP1 and LdUAP2
additional information
KT282116
knockdown of LdUAP2 or combined knockdown of LdUAP1 and LdUAP2
additional information
KT282117
knockdown of LdUAP2 or combined knockdown of LdUAP1 and LdUAP2
additional information
construction of Mycobacterium tuberculosis mutant strains overproducing GlmU allows determination of the contribution of the protein to mycobacterial entry into human neutrophils
additional information
-
construction of Mycobacterium tuberculosis mutant strains overproducing GlmU allows determination of the contribution of the protein to mycobacterial entry into human neutrophils
-
additional information
-
construction of Mycobacterium tuberculosis mutant strains overproducing GlmU allows determination of the contribution of the protein to mycobacterial entry into human neutrophils
-
additional information
the lesion mimic mutant spl29, regenerated from the cultivar Zhonghua 11, exhibits spotted leaves and rapid leaf senescence from the seedling stage throughout the rest of its life cycle, and no enzymatic activity in the spl29 mutant. Functional complementation with LOC_Os08g10600 in the spl29 mutant
additional information
-
the lesion mimic mutant spl29, regenerated from the cultivar Zhonghua 11, exhibits spotted leaves and rapid leaf senescence from the seedling stage throughout the rest of its life cycle, and no enzymatic activity in the spl29 mutant. Functional complementation with LOC_Os08g10600 in the spl29 mutant
-
additional information
for industrial applications, activity needs to be increased without decreasing thermostability. To enhance this activity, mutations are introduced into the amino acid residues located within the predicted reaction centre by targeted mutagenesis. All 12 mutant ST0452 proteins show no decrease in thermostability. Among them, six mutant proteins are found to have increased UDP-N-acetylglucosamine diphosphorylase activity under optimal reaction conditions with sufficient substrates or an appropriate metal ion
additional information
construction of expression vectors encoding a series of ST0452 C-terminal deletion mutants with hexahistidine tags at their C-termini, designated pST0452(DC005)H, pST0452(DC011)H, pST0452(DC021)H, pST0452(DC031)H, pST0452(DC041) H, pST0452(DC051)H, pST0452(DC071)H, pST0452 (DC121)H and pST0452(DC171)H. The deletion mutants retain the same tertiary structures as the wild-type ST0452 protein
additional information
-
construction of expression vectors encoding a series of ST0452 C-terminal deletion mutants with hexahistidine tags at their C-termini, designated pST0452(DC005)H, pST0452(DC011)H, pST0452(DC021)H, pST0452(DC031)H, pST0452(DC041) H, pST0452(DC051)H, pST0452(DC071)H, pST0452 (DC121)H and pST0452(DC171)H. The deletion mutants retain the same tertiary structures as the wild-type ST0452 protein
additional information
N-acetyl-D-glucosamine-1-phosphate uridylyltransferase activity of the mutant enzyme deletion mutant lacking the 170-residue C-terminal domain remains in the truncated enzyme after 5 min of heating at 65 °C but is completely removed by treatment over 70°C
additional information
ST0452 proteins exhibiting a further increase in activity are created using a site saturation mutagenesis strategy at the 97th position. Kinetic analyses show that the increased activities of the mutant proteins are principally due to increased apparent kcat values. Nine double-mutant ST0452 proteins are generated with the intent of obtaining enzymes exhibiting a further increase in catalysis, but all show less than 15% of the wild-type N-acetyl-D-glucosamine-1-phosphate uridyltransferase (GlcNAc-1-P UTase) activity. The Y97A mutant exhibits the highest activity of the single-mutant proteins. Analysis of mutant ST0452 proteins generated using a site saturation mutagenesis strategy at the 97th position, overview
additional information
-
ST0452 proteins exhibiting a further increase in activity are created using a site saturation mutagenesis strategy at the 97th position. Kinetic analyses show that the increased activities of the mutant proteins are principally due to increased apparent kcat values. Nine double-mutant ST0452 proteins are generated with the intent of obtaining enzymes exhibiting a further increase in catalysis, but all show less than 15% of the wild-type N-acetyl-D-glucosamine-1-phosphate uridyltransferase (GlcNAc-1-P UTase) activity. The Y97A mutant exhibits the highest activity of the single-mutant proteins. Analysis of mutant ST0452 proteins generated using a site saturation mutagenesis strategy at the 97th position, overview
additional information
all proteins substituted at position 146 have drastically decreased activities, whereas several proteins substituted at position 80 show higher GlcNAc-1-P UTase activity, compared to that of the wild-type protein
additional information
-
all proteins substituted at position 146 have drastically decreased activities, whereas several proteins substituted at position 80 show higher GlcNAc-1-P UTase activity, compared to that of the wild-type protein
additional information
-
for industrial applications, activity needs to be increased without decreasing thermostability. To enhance this activity, mutations are introduced into the amino acid residues located within the predicted reaction centre by targeted mutagenesis. All 12 mutant ST0452 proteins show no decrease in thermostability. Among them, six mutant proteins are found to have increased UDP-N-acetylglucosamine diphosphorylase activity under optimal reaction conditions with sufficient substrates or an appropriate metal ion
-
additional information
-
all proteins substituted at position 146 have drastically decreased activities, whereas several proteins substituted at position 80 show higher GlcNAc-1-P UTase activity, compared to that of the wild-type protein
-
additional information
-
ST0452 proteins exhibiting a further increase in activity are created using a site saturation mutagenesis strategy at the 97th position. Kinetic analyses show that the increased activities of the mutant proteins are principally due to increased apparent kcat values. Nine double-mutant ST0452 proteins are generated with the intent of obtaining enzymes exhibiting a further increase in catalysis, but all show less than 15% of the wild-type N-acetyl-D-glucosamine-1-phosphate uridyltransferase (GlcNAc-1-P UTase) activity. The Y97A mutant exhibits the highest activity of the single-mutant proteins. Analysis of mutant ST0452 proteins generated using a site saturation mutagenesis strategy at the 97th position, overview
-
additional information
-
N-acetyl-D-glucosamine-1-phosphate uridylyltransferase activity of the mutant enzyme deletion mutant lacking the 170-residue C-terminal domain remains in the truncated enzyme after 5 min of heating at 65 °C but is completely removed by treatment over 70°C
-
additional information
-
all proteins substituted at position 146 have drastically decreased activities, whereas several proteins substituted at position 80 show higher GlcNAc-1-P UTase activity, compared to that of the wild-type protein
-
additional information
-
all proteins substituted at position 146 have drastically decreased activities, whereas several proteins substituted at position 80 show higher GlcNAc-1-P UTase activity, compared to that of the wild-type protein
-
additional information
-
all proteins substituted at position 146 have drastically decreased activities, whereas several proteins substituted at position 80 show higher GlcNAc-1-P UTase activity, compared to that of the wild-type protein
-
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Mengin-Lecreulx, D.; van Heijenoort, J.
Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis
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Purification of uridine diphosphoacetylglucosamine pyrophosphorylase from sheep brain
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Uridine diphosphoacetylglucosamine pyrophosphorylase
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Saccharomyces cerevisiae, Neurospora crassa
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Identification of the gonococcal glmU gene encoding the enzyme N-acetylglucosamine 1-phosphate uridyltransferase involved in the synthesis of UDP-GlcNAc
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Neisseria gonorrhoeae (Q50986)
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Purification to homogeneity and properties of UDP-GlcNAc (GalNAc) pyrophosphorylase
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Escherichia coli
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Purification and characterization of UDP-N-acetylglucosamine pyrophosphorylase from encysting Giardia
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Mio, T.; Yabe, T.; Arisawa, M.; Yamada-Okabe, H.
The eukaryotic UDP-N-acetylglucosamine pyrophosphorylases. Gene cloning, protein expression, and catalytic mechanism
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Homo sapiens, Candida albicans (O74933), Candida albicans, Saccharomyces cerevisiae (P43123), Saccharomyces cerevisiae
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A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase specificity from UDP-GalNAc to UDP-GlcNAc
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Homo sapiens, Sus scrofa
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Identification and modification of the uridine-binding site of the UDP-GalNAc (GlcNAc) pyrophosphorylase
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Homo sapiens
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Bulik, D.A.; van Ophem, P.; Manning, J.M.; Shen, Z.; Newburg, D.S.; Jarroll, E.L.
UDP-N-acetylglucosamine pyrophosphorylase, a key enzyme in encysting Giardia, is allosterically regulated
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275
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Giardia intestinalis
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Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture
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276
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Escherichia coli (P0ACC7), Streptococcus pneumoniae (Q97R46), Streptococcus pneumoniae
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Shao, J.; Zhang, J.; Nahalka, J.; Wang, P.G.
Biocatalytic synthesis of uridine 5'-diphosphate N-acetylglucosamine by multiple enzymes co-immobilized on agarose beads
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2002
Escherichia coli
-
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Olsen, L.R.; Roderick, S.L.
Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites
Biochemistry
40
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2001
Escherichia coli (P0ACC7)
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Kostrewa, D.; D'Arcy, A.; Takacs, B.; Kamber, M.
Crystal structures of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, in apo form at 2.33 A resolution and in complex with UDP-N-acetylglucosamine and Mg(2+) at 1.96 A resolution
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305
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2001
Streptococcus pneumoniae (Q97R46)
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Brown, K.; Pompeo, F.; Dixon, S.; Mengin-Lecreulx, D.; Cambillau, C.; Bourne, Y.
Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily
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Escherichia coli
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Giardia intestinalis: molecular characterization of UDP-N-acetylglucosamine pyrophosphorylase
Gene
357
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2005
Giardia intestinalis (Q8MUP8), Giardia intestinalis
brenda
Mok, M.T.; Edwards, M.R.
Kinetic and physical characterization of the inducible UDP-N-acetylglucosamine pyrophosphorylase from Giardia intestinalis
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280
39363-39372
2005
Giardia intestinalis (Q8MUP8), Giardia intestinalis
brenda
Zhang, Z.; Tsujimura, M.; Akutsu, J.; Sasaki, M.; Tajima, H.; Kawarabayasi, Y.
Identification of an extremely thermostable enzyme with dual sugar-1-phosphate nucleotidylyltransferase activities from an acidothermophilic archaeon, Sulfolobus tokodaii strain 7
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280
9698-9705
2005
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii 7 (Q975F9)
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Purification, crystallization and preliminary X-ray diffraction studies of UDP-N-acetylglucosamine pyrophosphorylase from Candida albicans
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62
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2006
Candida albicans
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Maruyama, D.; Nishitani, Y.; Nonaka, T.; Kita, A.; Fukami, T.A.; Mio, T.; Yamada-Okabe, H.; Yamada-Okabe, T.; Miki, K.
Crystal structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans and catalytic reaction mechanism
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282
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Candida albicans
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Schimmelpfeng, K.; Strunk, M.; Stork, T.; Klaembt, C.
Mummy encodes an UDP-N-acetylglucosamine-dipohosphorylase and is required during Drosophila dorsal closure and nervous system development
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2006
Drosophila melanogaster
brenda
Yin, J.; Garen, C.R.; Cherney, M.M.; Cherney, L.T.; James, M.N.
Expression, purification and preliminary crystallographic analysis of N-acetylglucosamine-1-phosphate uridylyltransferase from Mycobacterium tuberculosis
Acta Crystallogr. Sect. F
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2008
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
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Guan, W.; Cai, L.; Fang, J.; Wu, B.; George Wang, P.
Enzymatic synthesis of UDP-GlcNAc/UDP-GalNAc analogs using N-acetylglucosamine 1-phosphate uridyltransferase (GlmU)
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6976-6978
2009
Escherichia coli
brenda
Mochalkin, I.; Lightle, S.; Narasimhan, L.; Bornemeier, D.; Melnick, M.; Vanderroest, S.; McDowell, L.
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Kinetic properties of Mycobacterium tuberculosis bifunctional GlmU
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193
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Min, J.; Lin, D.; Zhang, Q.; Zhang, J.; Yu, Z.
Structure-based virtual screening of novel inhibitors of the uridyltransferase activity of Xanthomonas oryzae pv. oryzae GlmU
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53
150-158
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Jagtap, P.K.; Soni, V.; Vithani, N.; Jhingan, G.D.; Bais, V.S.; Nandicoori, V.K.; Prakash, B.
Substrate bound crystal structures reveal features unique to Mycobacterium tuberculosis N-acetyl-glucosamine-1-phosphate uridyltransferase and a catalytic mechanism for acetyltransfer
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287
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Mycobacterium tuberculosis (P9WMN3), Mycobacterium tuberculosis
brenda
Yang, T.; Echols, M.; Martin, A.; Bar-Peled, M.
Identification and characterization of a strict and a promiscuous N-acetylglucosamine-1-P uridylyltransferase in Arabidopsis
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430
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Arabidopsis thaliana (O64765), Arabidopsis thaliana (Q940S3)
brenda
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Structure-based drug design studies of UDP-N-acetylglucosamine pyrophosphosrylase, a key enzyme for the control of witches broom disease
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7
48
2013
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Both UDP N-acetylglucosamine pyrophosphorylases of Tribolium castaneum are critical for molting, survival and fecundity
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41
42-50
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Escherichia coli (P0ACC7), Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 (Q975F9), Escherichia coli K12 (P0ACC7)
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Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7 (Q975F9), Sulfurisphaera tokodaii DSM 16993 (Q975F9), Sulfurisphaera tokodaii JCM 10545 (Q975F9), Sulfurisphaera tokodaii NBRC 100140 (Q975F9)
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Candida albicans (O74933), Mycobacterium tuberculosis (P9WMN3), Mycobacterium tuberculosis H37Rv (P9WMN3)
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Palaka, B.K.; Velmurugan Ilavarasi, A.; Sapam, T.D.; Kotapati, K.V.; Nallala, V.S.; Khan, M.B.; Ampasala, D.R.
Molecular cloning, gene expression analysis, and in silico characterization of UDP-N-acetylglucosamine pyrophosphorylase from Bombyx mori
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Bombyx mori (A0A089PRC4), Bombyx mori
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Patel, H.M.; Palkar, M.; Karpoormath, R.
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Mycobacterium tuberculosis (P9WMN3), Mycobacterium tuberculosis H37Rv (P9WMN3), Mycobacterium tuberculosis ATCC 25618 (P9WMN3)
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Chen, X.; Raimi, O.G.; Ferenbach, A.T.; van Aalten, D.M.F.
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Homo sapiens (Q16222)
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Braden, L.; Michaud, D.; Igboeli, O.O.; Dondrup, M.; Hamre, L.; Dalvin, S.; Purcell, S.L.; Kongshaug, H.; Eichner, C.; Nilsen, F.; Fast, M.D.
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Lepeophtheirus salmonis
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Sharma, R.; Lambu, M.R.; Jamwal, U.; Rani, C.; Chib, R.; Wazir, P.; Mukherjee, D.; Chaubey, A.; Khan, I.A.
Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) inhibitory activity of terreic acid isolated from Aspergillus terreus
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342-353
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Escherichia coli (P0ACC7), Escherichia coli ATCC 25922 (P0ACC7)
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Debets, M.F.; Tastan, O.Y.; Wisnovsky, S.P.; Malaker, S.A.; Angelis, N.; Moeckl, L.K.R.; Choi, J.; Flynn, H.; Wagner, L.J.S.; Bineva-Todd, G.; Antonopoulos, A.; Cioce, A.; Browne, W.M.; Li, Z.; Briggs, D.C.; Douglas, H.L.; Hess, G.T.; Agbay, A.J.; Roustan, C.; Kjaer, S.; Haslam, S.M.; Snijders, A.P.; Bassik, M.C.; , M.
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Homo sapiens (Q16222)
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