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Literature summary extracted from

  • 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 (2012), Eur. J. Med. Chem., 53, 150-158.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.23 homology modeling of structure based on Haemophilus influenzae enzyme, PDB entry 2V0K Xanthomonas oryzae pv. oryzae

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.23 luteolin minimal inhibitory concentration for growth of Xanthomonas oryzae pv. oryzae, 186 microg/ml Xanthomonas oryzae pv. oryzae
2.7.7.23 N'-[(4-chloro-3,5-dimethylphenoxy)acetyl]-2,4-dihydroxybenzohydrazide minimal inhibitory concentration for growth of Xanthomonas oryzae pv. oryzae, 420 microg/ml Xanthomonas oryzae pv. oryzae
2.7.7.23 N'1,N'6-bis[2-(naphthalen-2-yloxy)acetyl]hexanedihydrazide minimal inhibitory concentration for growth of Xanthomonas oryzae pv. oryzae, 302 microg/ml Xanthomonas oryzae pv. oryzae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.157 acetyl-CoA + alpha-D-glucosamine 1-phosphate Xanthomonas oryzae
-
 CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.157 Xanthomonas oryzae
-
 pv. oryzae
-
2.7.7.23 Xanthomonas oryzae pv. oryzae Q2P7P9 bifunctional UDP-N-acetylglucosamine diphosphorylase, EC 2.7.7.23, and glucosamine-1-phosphate N-acetyltransferase, EC 2.3.1.157
-
2.7.7.23 Xanthomonas oryzae pv. oryzae MAFF 311018 Q2P7P9 bifunctional UDP-N-acetylglucosamine diphosphorylase, EC 2.7.7.23, and glucosamine-1-phosphate N-acetyltransferase, EC 2.3.1.157
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.157 acetyl-CoA + alpha-D-glucosamine 1-phosphate
-
 Xanthomonas oryzae CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
2.7.7.23 N-acetyl-alpha-D-glucosamine 1-phosphate + UTP
-
 Xanthomonas oryzae pv. oryzae UDP-N-acetyl-alpha-D-glucosamine + diphosphate
-
 ?
2.7.7.23 N-acetyl-alpha-D-glucosamine 1-phosphate + UTP
-
 Xanthomonas oryzae pv. oryzae MAFF 311018 UDP-N-acetyl-alpha-D-glucosamine + diphosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.157 GlmU
-
 Xanthomonas oryzae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.7.23 0.00044
-
 luteolin substrate N-acetyl-alpha-D-glucosamine 1-phosphate, pH 7.5, 37°C Xanthomonas oryzae pv. oryzae
2.7.7.23 0.00099
-
 luteolin substrate UTP, pH 7.5, 37°C Xanthomonas oryzae pv. oryzae
2.7.7.23 0.0081
-
 N'1,N'6-bis[2-(naphthalen-2-yloxy)acetyl]hexanedihydrazide substrate N-acetyl-alpha-D-glucosamine 1-phosphate, pH 7.5, 37°C Xanthomonas oryzae pv. oryzae
2.7.7.23 0.0081
-
 N'1,N'6-bis[2-(naphthalen-2-yloxy)acetyl]hexanedihydrazide substrate UTP, pH 7.5, 37°C Xanthomonas oryzae pv. oryzae
2.7.7.23 0.0089
-
 N'-[(4-chloro-3,5-dimethylphenoxy)acetyl]-2,4-dihydroxybenzohydrazide substrate UTP, pH 7.5, 37°C Xanthomonas oryzae pv. oryzae
2.7.7.23 0.0194
-
 N'-[(4-chloro-3,5-dimethylphenoxy)acetyl]-2,4-dihydroxybenzohydrazide substrate N-acetyl-alpha-D-glucosamine 1-phosphate, pH 7.5, 37°C Xanthomonas oryzae pv. oryzae

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.7.7.23 0.00081
-
 pH 7.5, 37°C Xanthomonas oryzae pv. oryzae luteolin
2.7.7.23 0.014
-
 pH 7.5, 37°C Xanthomonas oryzae pv. oryzae N'1,N'6-bis[2-(naphthalen-2-yloxy)acetyl]hexanedihydrazide
2.7.7.23 0.023
-
 pH 7.5, 37°C Xanthomonas oryzae pv. oryzae N'-[(4-chloro-3,5-dimethylphenoxy)acetyl]-2,4-dihydroxybenzohydrazide

General Information

EC Number General Information Comment Organism
2.3.1.157 physiological function the bifunctional enzyme N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, catalyzes two-step formation of UDP-GlcNAc, an important precursor in bacterial peptidoglycan and lipopolysaccharide biosynthesis, which are important constituents of the cell wall of both Gram-positive and Gram-negative bacteria. The first activity of GlmU, the C-terminal domain (acetyltransferase), catalyzes the formation of N-acetylglucosamine-1-phosphate from glucosamine-1-phosphate using acetyl-CoA as the acetyl donor. The second activity of GlmU, the N-terminal and rate-limiting domain (uridyltransferase), catalyzes the formation of UDP-GlcNAc from GlcNAc-1-phosphate and uridine triphosphate, UTP Xanthomonas oryzae