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Information on EC 2.7.7.23 - UDP-N-acetylglucosamine diphosphorylase and Organism(s) Streptococcus pneumoniae serotype 4 and UniProt Accession Q97R46

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IUBMB Comments
Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase [3,4,6]. The enzyme from plants and animals is also active toward N-acetyl-alpha-D-galactosamine 1-phosphate (cf. EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase) [5,7], while the bacterial enzyme shows low activity toward that substrate .
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Streptococcus pneumoniae serotype 4
UNIPROT: Q97R46
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Word Map
The enzyme appears in selected viruses and cellular organisms
Synonyms
udp-n-acetylglucosamine pyrophosphorylase, lmuap1, glmumtb, glcnac-1-p utase, spl29, udp-n-acetylglucosamine pyrophosphorylase (uap), udp-n-acetylglucosamine pyrophosphorylase 1, n-acetylglucosamine 1-phosphate uridyltransferase, agx-1, udp-n-acetylhexosamine pyrophosphorylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylglucosamine 1-phosphate uridylyltransferase
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GlmU
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UDP-GlcNAc pyrophosphorylase
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UDP-HexNAc pyrophosphorylase
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UDPacetylglucosamine pyrophosphorylase
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uridine diphosphate-N-acetylglucosamine pyrophosphorylase
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uridine diphosphoacetylglucosamine phosphorylase
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uridine diphosphoacetylglucosamine pyrophosphorylase
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UTP:2-acetamido-2-deoxy-alpha-D-glucose-1-phosphate uridylyltransferase
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Ydl103c protein
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
UTP:N-acetyl-alpha-D-glucosamine-1-phosphate uridylyltransferase
Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase [3,4,6]. The enzyme from plants and animals is also active toward N-acetyl-alpha-D-galactosamine 1-phosphate (cf. EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase) [5,7], while the bacterial enzyme shows low activity toward that substrate [4].
CAS REGISTRY NUMBER
COMMENTARY hide
9023-06-7
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