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evolution
N-acetyl-glucosamine-1-phosphate uridyltransferase, GlmU, is exclusive to prokaryotes, conserved both in Gram positive and Gram negative bacteria
evolution
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the GlmU proteins encoded by Yersinia pestis and Yersinia pseudotuberculosis are identical in amino acid sequence
evolution
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the GlmU proteins encoded by Yersinia pestis and Yersinia pseudotuberculosis are identical in amino acid sequence
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malfunction
Deleting the C-terminal tail, i.e. residues 457-495, of GlmUMtb that provides these residues abolishes all acetyltransferase activity
malfunction
GlmUMtb depletion perturbs cell wall structure and affects the bacterial survival in normoxia, overview
malfunction
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GlmUMtb depletion perturbs cell wall structure and affects the bacterial survival in normoxia, overview
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malfunction
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GlmUMtb depletion perturbs cell wall structure and affects the bacterial survival in normoxia, overview
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metabolism
N-acetyl-glucosamine-1-phosphate uridyltransferase, GlmU, is a bifunctional enzyme involved in bacterial cell wall synthesis
metabolism
the enzymeis involved in the UDP-N-acetylglucosamine synthesis pathway, overview
metabolism
the bifunctional enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan
metabolism
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the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
metabolism
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the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
metabolism
the enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan
metabolism
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pathway and metabolism of UDP-N-acetylglucosamine in prokaryotes and eukaryotes, overview
metabolism
pathway and metabolism of UDP-N-acetylglucosamine in prokaryotes and eukaryotes, overview
metabolism
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the bifunctional enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan
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metabolism
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the enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan
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metabolism
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the enzymeis involved in the UDP-N-acetylglucosamine synthesis pathway, overview
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metabolism
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the enzyme is involved in the cell wall biosynthesis of Gram-negative organisms
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metabolism
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pathway and metabolism of UDP-N-acetylglucosamine in prokaryotes and eukaryotes, overview
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physiological function
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essentiality of GlmU to mycobacterial survival
physiological function
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GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
physiological function
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GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
physiological function
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GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
physiological function
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GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
physiological function
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GlmU is a bifunctional enzyme with acetyltransferase activity in C-terminus, residues 251-495, and uridyltransferase activity in N-terminus, and it is involved in the biosynthesis of glycosyl donor UDP-N-acetylglucosamine
physiological function
GlmU is involved in the biosynthesis of UDP-N-acetylglucosamine-1-phosphate. It is a bifunctional protein with two independent active sites catalyzing acetyl transfer and uridyl transfer reactions on glucosamine-1-phosphate. It synthesizes two key intermediates of cell wall biosynthesis pathways, viz. N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc. The acetyltransferase activity is catalyzed by the C-terminal domain. It is essential for the growth of the organism
physiological function
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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
physiological function
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the C- and N-terminal domains of bifunctional enzyme mycobacterial glucosamine 1-phosphate N-acetyltransferase/N-acetylglucosamine-1-phosphate uridyltransferase catalyze acetyltransferase and uridyltransferase (cf. EC 2.7.7.23) activities, respectively, and the final product is involved in peptidoglycan synthesis
physiological function
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the C-terminal domain of bifunctional GlmU catalyzes the transfer of an acetyl group from acetyl coenzyme A to glucosamine-1-phosphate to produce N-acetylglucosamine-1-phosphate. In the second step, the N-terminal domain of GlmU catalyzes the transfer of uridyl monophosphate from UTP to acetylglucosamine-1-phosphate to produce UDP-GlcNAc and diphosphate
physiological function
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the C-terminal domain of bifunctional GlmU catalyzes the transfer of an acetyl group from acetyl coenzyme A to glucosamine-1-phosphate to produce N-acetylglucosamine-1-phosphate. In the second step, the N-terminal domain of GlmU catalyzes the transfer of uridyl monophosphate from UTP to acetylglucosamine-1-phosphate to produce UDP-GlcNAc and diphosphate
physiological function
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the C-terminal domain of bifunctional GlmU catalyzes the transfer of an acetyl group from acetyl coenzyme A to glucosamine-1-phosphate to produce N-acetylglucosamine-1-phosphate. In the second step, the N-terminal domain of GlmU catalyzes the transfer of uridyl monophosphate from UTP to acetylglucosamine-1-phosphate to produce UDP-GlcNAc and diphosphate
physiological function
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the C-terminal domain of bifunctional GlmU catalyzes the transfer of an acetyl group from acetyl coenzyme A to glucosamine-1-phosphate to produce N-acetylglucosamine-1-phosphate. In the second step, the N-terminal domain of GlmU catalyzes the transfer of uridyl monophosphate from UTP to acetylglucosamine-1-phosphate to produce UDP-GlcNAc and diphosphate
physiological function
because the ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
physiological function
absence of GlmU leads to extensive perturbation of bacterial morphology and substantial reduction in cell wall thickness under normoxic as well as hypoxic conditions. The acetyl- and uridyl-transferase activities of GlmU are independently essential for bacterial survival in vitro, and GlmU is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. Depletion of GlmU from infected murine lungs, four weeks post infection, leads to significant reduction in the bacillary load
physiological function
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme involved in bacterial cell wall synthesis and is exclusive to prokaryotes. The enzyme is regulated by PknB via phosphorylation at Thr418 causing downregulation of acetyltransferase
physiological function
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively. Final product of GlmU catalyzed reaction, uridine-diphospho-N-acetylglucosamine (UDP-GlcNAc), acts as sugar donor providing GlcNAc residues in the synthesis of peptidoglycan and a disaccharide linker (D-N-GlcNAc-1-rhamnose), the key structural components of Mycobacterium tuberculosis cell wall
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
physiological function
the archaeal enzyme's high GalN-1-P AcTase activity, which is not detected on the bacterial and eukaryotic similar enzymes, supports the production of the UDP-GalNAc in archaeal cells
physiological function
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the bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase enzyme GlmU is an essential gene in Yersinia
physiological function
the enzyme is one of the pathogen proteins that bind to human interleukin-8, IL-8. The binding interaction of mycobacterial proteins AtsG, GlmU and SahH with human IL-8 may indicate that these proteins participate in the modulation of the early events of infection with tubercle bacilli and could affect pathogen attachment to target cells. Interleukin-8 belongs to the family of CXC chemokines and functions as a chemoattractant and activator of different subsets of leukocytes
physiological function
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GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
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physiological function
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because the ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon
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physiological function
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the archaeal enzyme's high GalN-1-P AcTase activity, which is not detected on the bacterial and eukaryotic similar enzymes, supports the production of the UDP-GalNAc in archaeal cells
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physiological function
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the enzyme is one of the pathogen proteins that bind to human interleukin-8, IL-8. The binding interaction of mycobacterial proteins AtsG, GlmU and SahH with human IL-8 may indicate that these proteins participate in the modulation of the early events of infection with tubercle bacilli and could affect pathogen attachment to target cells. Interleukin-8 belongs to the family of CXC chemokines and functions as a chemoattractant and activator of different subsets of leukocytes
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physiological function
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absence of GlmU leads to extensive perturbation of bacterial morphology and substantial reduction in cell wall thickness under normoxic as well as hypoxic conditions. The acetyl- and uridyl-transferase activities of GlmU are independently essential for bacterial survival in vitro, and GlmU is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. Depletion of GlmU from infected murine lungs, four weeks post infection, leads to significant reduction in the bacillary load
-
physiological function
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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
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physiological function
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N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively. Final product of GlmU catalyzed reaction, uridine-diphospho-N-acetylglucosamine (UDP-GlcNAc), acts as sugar donor providing GlcNAc residues in the synthesis of peptidoglycan and a disaccharide linker (D-N-GlcNAc-1-rhamnose), the key structural components of Mycobacterium tuberculosis cell wall
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physiological function
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the enzyme is one of the pathogen proteins that bind to human interleukin-8, IL-8. The binding interaction of mycobacterial proteins AtsG, GlmU and SahH with human IL-8 may indicate that these proteins participate in the modulation of the early events of infection with tubercle bacilli and could affect pathogen attachment to target cells. Interleukin-8 belongs to the family of CXC chemokines and functions as a chemoattractant and activator of different subsets of leukocytes
-
physiological function
-
absence of GlmU leads to extensive perturbation of bacterial morphology and substantial reduction in cell wall thickness under normoxic as well as hypoxic conditions. The acetyl- and uridyl-transferase activities of GlmU are independently essential for bacterial survival in vitro, and GlmU is also essential for mycobacterial survival in THP-1 cells as well as in guinea pigs. Depletion of GlmU from infected murine lungs, four weeks post infection, leads to significant reduction in the bacillary load
-
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
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physiological function
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the bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase enzyme GlmU is an essential gene in Yersinia
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physiological function
-
GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
-
physiological function
-
the archaeal enzyme's high GalN-1-P AcTase activity, which is not detected on the bacterial and eukaryotic similar enzymes, supports the production of the UDP-GalNAc in archaeal cells
-
physiological function
-
GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
-
physiological function
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GlmU is a bifunctional enzyme that is essential for bacterial growth, converting D-glucosamine 1-phosphate into UDPGlcNAc via acetylation and subsequent uridyl transfer
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additional information
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analysis of structures of GlmUMtb bound to substrates of the acetyl transfer reaction
additional information
analysis of structures of GlmUMtb bound to substrates of the acetyl transfer reaction
additional information
the C-terminal tail region of the ST0452 protein might be important for recognition of the multiple substrates for amino-sugar-1-P AcTase activity. The ST0452 protein contains only two Cys residues, it is unlikely that Cys-Cys bonds contribute to its thermostability. Residue Asn331 in the ST0452 protein is essential for the GalN-1-P AcTase activity, but it is much less important and not essential for the GlcN-1-P AcTase activity. The C-terminal residues of the ST0452 protein enhance the turnover rate of its GalN-1-P AcTase catalytic activity and slightly suppress substrate binding. Residue H308 is essential for both amino-sugar-1-P AcTase activities of the ST0452 protein
additional information
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the C-terminal tail region of the ST0452 protein might be important for recognition of the multiple substrates for amino-sugar-1-P AcTase activity. The ST0452 protein contains only two Cys residues, it is unlikely that Cys-Cys bonds contribute to its thermostability. Residue Asn331 in the ST0452 protein is essential for the GalN-1-P AcTase activity, but it is much less important and not essential for the GlcN-1-P AcTase activity. The C-terminal residues of the ST0452 protein enhance the turnover rate of its GalN-1-P AcTase catalytic activity and slightly suppress substrate binding. Residue H308 is essential for both amino-sugar-1-P AcTase activities of the ST0452 protein
additional information
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the catalytic mechanism operative in GlmUMtb performs a SN2 reaction, His374 and Asn397 act as catalytic residues by enhancing the nucleophilicity of the attacking amino group of glucosamine 1-phosphate. Ser416 and Trp460, on a short helix, provide important interactions for substrate binding. The enzyme shows an uncommon mode of binding with acetyl-CoA. GlmU from Mycobacterium tuberculosis possesses a unique 30-residue extension at the C-terminus. The adenine base of acetyl-CoA bound to GlmUMtb is buried at the interface of two monomers of the trimer
additional information
the catalytic mechanism operative in GlmUMtb performs a SN2 reaction, His374 and Asn397 act as catalytic residues by enhancing the nucleophilicity of the attacking amino group of glucosamine 1-phosphate. Ser416 and Trp460, on a short helix, provide important interactions for substrate binding. The enzyme shows an uncommon mode of binding with acetyl-CoA. GlmU from Mycobacterium tuberculosis possesses a unique 30-residue extension at the C-terminus. The adenine base of acetyl-CoA bound to GlmUMtb is buried at the interface of two monomers of the trimer
additional information
-
the C-terminal tail region of the ST0452 protein might be important for recognition of the multiple substrates for amino-sugar-1-P AcTase activity. The ST0452 protein contains only two Cys residues, it is unlikely that Cys-Cys bonds contribute to its thermostability. Residue Asn331 in the ST0452 protein is essential for the GalN-1-P AcTase activity, but it is much less important and not essential for the GlcN-1-P AcTase activity. The C-terminal residues of the ST0452 protein enhance the turnover rate of its GalN-1-P AcTase catalytic activity and slightly suppress substrate binding. Residue H308 is essential for both amino-sugar-1-P AcTase activities of the ST0452 protein
-
additional information
-
the C-terminal tail region of the ST0452 protein might be important for recognition of the multiple substrates for amino-sugar-1-P AcTase activity. The ST0452 protein contains only two Cys residues, it is unlikely that Cys-Cys bonds contribute to its thermostability. Residue Asn331 in the ST0452 protein is essential for the GalN-1-P AcTase activity, but it is much less important and not essential for the GlcN-1-P AcTase activity. The C-terminal residues of the ST0452 protein enhance the turnover rate of its GalN-1-P AcTase catalytic activity and slightly suppress substrate binding. Residue H308 is essential for both amino-sugar-1-P AcTase activities of the ST0452 protein
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