Application | Comment | Organism |
---|---|---|
medicine | GlmUMtb is a strong candidate for intervention measures against established tuberculosis infections | Mycobacterium tuberculosis |
Cloned (Comment) | Organism |
---|---|
gene glmU, recombinant expression of N-terminally FLAG-tagged enzyme | Mycobacterium tuberculosis |
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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WMN3 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WMN3 | - |
- |
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 | Comment | Organism |
---|---|---|
GlmU | - |
Mycobacterium tuberculosis |
N-acetylglucosamine-1-phosphate uridyltransferase | - |
Mycobacterium tuberculosis |
Rv1018c | - |
Mycobacterium tuberculosis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Mycobacterium tuberculosis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Mycobacterium tuberculosis |
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 | 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 |