Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Application

EC Number Application Comment Organism
2.7.7.23 medicine potential target for antibacterial agents Streptococcus pneumoniae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.157 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
2.7.7.23
-
 Streptococcus pneumoniae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.1.157 Mg2+ required Streptococcus pneumoniae
2.7.7.23 Mg2+ cofactor Streptococcus pneumoniae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.157 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
-
 ?
2.7.7.23 diphosphate + UDP-N-acetyl-D-glucosamine Streptococcus pneumoniae amino sugar metabolism UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 r
2.7.7.23 diphosphate + UDP-N-acetyl-D-glucosamine Streptococcus pneumoniae involved in synthesis of peptidoglycan and lipopolysaccharide UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.157 Streptococcus pneumoniae Q97R46
-
-
2.7.7.23 Streptococcus pneumoniae Q97R46
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.157 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
-
 ?
2.3.1.157 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
-
 ?
2.7.7.23 diphosphate + UDP-N-acetyl-D-glucosamine
-
 Streptococcus pneumoniae UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 r
2.7.7.23 diphosphate + UDP-N-acetyl-D-glucosamine amino sugar metabolism Streptococcus pneumoniae UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 r
2.7.7.23 diphosphate + UDP-N-acetyl-D-glucosamine involved in synthesis of peptidoglycan and lipopolysaccharide Streptococcus pneumoniae UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 r

Subunits

EC Number Subunits Comment Organism
2.7.7.23 trimer
-
 Streptococcus pneumoniae

Synonyms

EC Number Synonyms Comment Organism
2.3.1.157 GlmU bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase Streptococcus pneumoniae
2.3.1.157 N-acetylglucosamine-1-phosphate uridyltransferase bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase Streptococcus pneumoniae
2.7.7.23 More bifunctional enzyme with activity of: glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase Streptococcus pneumoniae