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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 + 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
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
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 + 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-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-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
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
-
-
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
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
-
-
-
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
?
-
-
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
-
?
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
-
-
-
r
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate
diphosphate + UDP-N-acetyl-alpha-D-galactosamine
-
-
-
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
-
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
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
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
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
-
-
-
-
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
-
-
?
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
?
-
-
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 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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(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
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-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
-
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-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
-
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
-
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 enzyme–substrate 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-(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-(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-[(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]benzamide
44% inhibition at 2 mM
N-[4-[(7-hydroxy-6-methoxyquinazolin-4-yl)amino]phenyl]benzamide
36% inhibition at 2 mM
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
-
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
[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
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

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
-
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
-
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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