Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.7.23 extracted from

  • Rani, C.; Mehra, R.; Sharma, R.; Chib, R.; Wazir, P.; Nargotra, A.; Khan, I.A.
    High-throughput screen identifies small molecule inhibitors targeting acetyltransferase activity of Mycobacterium tuberculosis GlmU (2015), Tuberculosis, 95, 664-677.
    View publication on PubMed
Search for more literature for 2.7.7.23

Cloned(Commentary)

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

Inhibitors

Inhibitors Comment Organism Structure
EDTA
-
 Mycobacterium tuberculosis
additional information no inhibition by 6624116, 5655606, 5810599, and 6012954 Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Mycobacterium tuberculosis
0.03
-
 UTP pH 7.5, 37°C, recombinant enzyme Mycobacterium tuberculosis
0.041
-
 N-acetyl-alpha-D-glucosamine 1-phosphate pH 7.5, 37°C, recombinant enzyme Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mycobacterium tuberculosis 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 ?
-
 ?
additional information Mycobacterium tuberculosis H37Rv 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 ?
-
 ?
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
-
 ?

Organism

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

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information 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 Mycobacterium tuberculosis ?
-
 ?
additional information 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 Mycobacterium tuberculosis H37Rv ?
-
 ?
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
-
 ?

Synonyms

Synonyms Comment Organism
GlmU
-
 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
7.5
-
 assay at Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
 Mycobacterium tuberculosis

General Information

General Information Comment Organism
metabolism the enzymeis involved in the UDP-N-acetylglucosamine synthesis pathway, overview Mycobacterium tuberculosis
physiological function N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyze 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 Mycobacterium tuberculosis