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Literature summary extracted from

  • Zhang, Z.; Bulloch, E.M.; Bunker, R.D.; Baker, E.N.; Squire, C.J.
    Structure and function of GlmU from Mycobacterium tuberculosis (2009), Acta Crystallogr. Sect. D, 65, 275-283.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.3.1.157 additional information MtGlmU has acetyltransferase activity in the absence of reducing agent and in the presence of a thiolreactive reagent (N-ethylmaleimide) Mycobacterium tuberculosis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.157 expressed in Escherichia coli as a His-tagged fusion protein Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.157 the crystal structures of MtGlmU in an unliganded form and in complexes in which either GlcNAc-1-P or UDP-GlcNAc occupies the uridyltransferase active site are determined using the sitting-drop vapour-diffusion method. These structures identify the active-site contacts between protein and ligands and suggest a ternary-complex mechanism of action for the GlmU uridyltransferase reaction Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.157 Mycobacterium tuberculosis P9WMN3
-
-
2.3.1.157 Mycobacterium tuberculosis H37Rv P9WMN3
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.157 using Ni-NTA chromatography. The His6 tag is cleaved by incubation with recombinant tobacco etch virus (rTEV) protease Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.157 D-glucosamine 1-phosphate + acetyl-CoA presence of acetyl-coenzyme A has an inhibitory effect on uridyltransferase activity of the bifunctional enzyme Mycobacterium tuberculosis N-acetyl-D-glucosamine 1-phosphate + CoA
-
 ?
2.3.1.157 D-glucosamine 1-phosphate + acetyl-CoA presence of acetyl-coenzyme A has an inhibitory effect on uridyltransferase activity of the bifunctional enzyme Mycobacterium tuberculosis H37Rv N-acetyl-D-glucosamine 1-phosphate + CoA
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.157 MtGlmU bifunctional enzyme also possesses the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase Mycobacterium tuberculosis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.157 37
-
 assay at Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.157 7.5
-
 assay at Mycobacterium tuberculosis