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Literature summary for 2.3.1.157 extracted from

  • 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 (2001), J. Mol. Biol., 305, 279-289.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
vapor-diffusion method, crystal structure of the enzyme in apo form at 2.33 A resolution, and in complex with UDP-N-acetyl glucosamine and the essential cofactor Mg2+ at 1.96 A resolution. In the crystal, the enzyme forms exact trimers, mainly through contacts between left-handed beta-sheet helix domains. UDP-N-acetylglucosamine and Mg2+ are bound at the uridyltransferase active site, which is in a closed form Streptococcus pneumoniae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Streptococcus pneumoniae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glucosamine 1-phosphate + acetyl-CoA Streptococcus pneumoniae the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine, which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathway N-acetyl-D-glucosamine 1-phosphate + CoA
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Organism

Organism UniProt Comment Textmining
Streptococcus pneumoniae Q97R46
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucosamine 1-phosphate + acetyl-CoA the bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase and performs the last two steps in the synthesis of UDP-N-acetylglucosamine, which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathway Streptococcus pneumoniae N-acetyl-D-glucosamine 1-phosphate + CoA
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D-glucosamine 1-phosphate + acetyl-CoA a mechanism is proposed in which the activation energy of the double negatively charged phosphorane transition state is lowered by charge compensation of Mg2+ and the side-chain of Lys22 Streptococcus pneumoniae N-acetyl-D-glucosamine 1-phosphate + CoA
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Synonyms

Synonyms Comment Organism
GlmU bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase Streptococcus pneumoniae
N-acetylglucosamine-1-phosphate uridyltransferase bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase Streptococcus pneumoniae