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Literature summary for 2.7.7.23 extracted from

  • Sharma, R.; Rani, C.; Mehra, R.; Nargotra, A.; Chib, R.; Rajput, V.; Kumar, S.; Singh, S.; Sharma, P.; Khan, I.
    Identification and characterization of novel small molecule inhibitors of the acetyltransferase activity of Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) (2015), Appl. Microbiol. Biotechnol., 100, 3071-3085.
    View publication on PubMed
Search for more literature for 2.7.7.23

Cloned(Commentary)

Cloned (Comment) Organism
gene glmU, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli 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 Escherichia coli ATCC 25922 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 ?
-
 ?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate Escherichia coli
-
 diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 ?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate Escherichia coli ATCC 25922
-
 diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ACC7 Escherichia coli K-12
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Escherichia coli ATCC 25922 P0ACC7 Escherichia coli K-12
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 Escherichia coli ?
-
 ?
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 Escherichia coli ATCC 25922 ?
-
 ?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 Escherichia coli diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 ?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 Escherichia coli ATCC 25922 diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 ?

Synonyms

Synonyms Comment Organism
GlmU
-
 Escherichia coli
N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
 assay at Escherichia coli

General Information

General Information Comment Organism
physiological function the product of the GlmU catalyzed reactions, UDP-N-acetylglucosamine, is a significant precursor for the peptidoglycan and LPS biosynthesis in Gram-positive and Gram-negative bacteria, respectively Escherichia coli