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Literature summary for 2.3.1.157 extracted from

  • Zhou, Y.; Yu, W.; Zheng, Q.; Xin, Y.; Ma, Y.
    Identification of amino acids involved in catalytic process of M. tuberculosis GlmU acetyltransferase (2012), Glycoconj. J., 29, 297-303.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene glmU, expression of N-terminally His-tagged wild-type GlmU and mutant GlmUs in Escherichia coli strain BL21(DE3) Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
E458A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, 86% of wild-type acetyltransferase activity is remaining Mycobacterium tuberculosis
H374A site-directed mutagenesis, the enzyme activity of the mutant is abolished by more than 90% of the wild-type acetyltransferase, and the affinity with the two substrates is completely lost Mycobacterium tuberculosis
K362A site-directed mutagenesis, the enzyme activity of the mutant is abolished by more than 90% of the wild-type acetyltransferase, and the affinity with the two substrates is completely lost Mycobacterium tuberculosis
K403A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, 27% of wild-type acetyltransferase activity is remaining Mycobacterium tuberculosis
N456A site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme, 67% of wild-type acetyltransferase activity is remaining Mycobacterium tuberculosis
R463A site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme Mycobacterium tuberculosis
S416A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, 65% of wild-type acetyltransferase activity is remaining Mycobacterium tuberculosis
S474A site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme Mycobacterium tuberculosis
W460A site-directed mutagenesis, the enzyme activity of the mutant is abolished by more than 90% of the wild-type acetyltransferase, and the affinity with the two substrates is completely lost Mycobacterium tuberculosis
Y398A site-directed mutagenesis, the enzyme activity of the mutant is abolished by more than 90% of the wild-type acetyltransferase, and the affinity with the two substrates is completely lost Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.008
-
alpha-D-glucosamine 1-phosphate pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant K403A Mycobacterium tuberculosis
0.044
-
alpha-D-glucosamine 1-phosphate pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant N456A Mycobacterium tuberculosis
0.056
-
acetyl-CoA pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant K403A Mycobacterium tuberculosis
0.06
-
acetyl-CoA pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant E458A Mycobacterium tuberculosis
0.061
-
alpha-D-glucosamine 1-phosphate pH and temperature not specified in the publication, recombinant His-tagged wild-type GlmU Mycobacterium tuberculosis
0.066
-
alpha-D-glucosamine 1-phosphate pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant E458A Mycobacterium tuberculosis
0.069
-
alpha-D-glucosamine 1-phosphate pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant R463A Mycobacterium tuberculosis
0.07
-
acetyl-CoA pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant S416A Mycobacterium tuberculosis
0.073
-
alpha-D-glucosamine 1-phosphate pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant S474A Mycobacterium tuberculosis
0.13
-
alpha-D-glucosamine 1-phosphate pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant S416A Mycobacterium tuberculosis
0.224
-
acetyl-CoA pH and temperature not specified in the publication, recombinant His-tagged wild-type GlmU Mycobacterium tuberculosis
0.242
-
acetyl-CoA pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant S474A Mycobacterium tuberculosis
0.304
-
acetyl-CoA pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant R463A Mycobacterium tuberculosis
0.343
-
acetyl-CoA pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant N456A Mycobacterium tuberculosis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
54100
-
x * 54100,, recombinant Histagged GlmU, SDS-PAGE Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + alpha-D-glucosamine 1-phosphate Mycobacterium tuberculosis
-
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
gene glmU
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally His-tagged wild-type GlmU and mutant GlmUs from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + alpha-D-glucosamine 1-phosphate
-
Mycobacterium tuberculosis CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
?

Subunits

Subunits Comment Organism
? x * 54100,, recombinant Histagged GlmU, SDS-PAGE Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
GlmU
-
Mycobacterium tuberculosis
GlmU acetyltransferase
-
Mycobacterium tuberculosis

General Information

General Information Comment Organism
physiological function 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 Mycobacterium tuberculosis