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Literature summary for 2.7.7.23 extracted from

  • Soni, V.; Upadhayay, S.; Suryadevara, P.; Samla, G.; Singh, A.; Yogeeswari, P.; Sriram, D.; Nandicoori, V.K.
    Depletion of M. tuberculosis GlmU from infected murine lungs effects the clearance of the pathogen (2015), PLoS Pathog., 11, e1005235.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.23

Application

Application Comment Organism
medicine GlmUMtb is a strong candidate for intervention measures against established tuberculosis infections Mycobacterium tuberculosis

Cloned(Commentary)

Cloned (Comment) Organism
gene glmU, recombinant expression of N-terminally FLAG-tagged enzyme Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
(Z)-4-(4-(benzyloxy)benzylidene)-2-(naphthalen-1-yl)oxazol-5(4H)-one i.e. Oxa33, synthesis of a specific GlmU inhibitor, molecular docking study, the inhibitor binds to an allosteric site of the uridyltransferase domain, overview. Oxa33 fails to inhibit cell growth even at concentrations as high as 0.150 mM. Tyr150, Glu250 and Arg 253 are in hydrogen bonding with carbonyl oxygen over the oxazole ring, while Leu144, Pro147, Phe148, Tyr150, Ala233, Ala236 and Leu247 participate in strong hydrophobic interactions with Oxa33 Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mycobacterium tuberculosis 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. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols ?
-
 ?
additional information Mycobacterium tuberculosis H37Rv 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. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols ?
-
 ?
additional information Mycobacterium tuberculosis ATCC 25618 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. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols ?
-
 ?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate Mycobacterium tuberculosis
-
 diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 ?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate Mycobacterium tuberculosis H37Rv
-
 diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 ?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate Mycobacterium tuberculosis ATCC 25618
-
 diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WMN3
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-
Mycobacterium tuberculosis H37Rv P9WMN3
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-

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. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols Mycobacterium tuberculosis ?
-
 ?
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. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols Mycobacterium tuberculosis H37Rv ?
-
 ?
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. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols Mycobacterium tuberculosis ATCC 25618 ?
-
 ?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 Mycobacterium tuberculosis diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 ?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 Mycobacterium tuberculosis H37Rv diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 ?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 Mycobacterium tuberculosis ATCC 25618 diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 ?

Synonyms

Synonyms Comment Organism
GlmU
-
 Mycobacterium tuberculosis
N-acetylglucosamine-1-phosphate uridyltransferase
-
 Mycobacterium tuberculosis
Rv1018c
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 Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Mycobacterium tuberculosis

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.00996
-
 pH 7.4, 37°C Mycobacterium tuberculosis (Z)-4-(4-(benzyloxy)benzylidene)-2-(naphthalen-1-yl)oxazol-5(4H)-one

General Information

General Information Comment Organism
malfunction GlmUMtb depletion perturbs cell wall structure and affects the bacterial survival in normoxia, overview Mycobacterium tuberculosis
physiological function the acetyl- and uridyltransferase activities of GlmUMtb are independently essential for bacterial survival in vitro, and GlmUMtb is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. The administration of Oxa33, a novel oxazolidine derivative that specifically inhibits GlmUMtb, to infected mice results in significant decrease in the bacillary load. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively Mycobacterium tuberculosis