Literature summary for 2.3.1.157 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.

Search for more literature for 2.3.1.157

Activating Compound

Activating Compound	Comment	Organism	Structure
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)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

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

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	-	?
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

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

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Release 2023.1 (January 2023)