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Literature summary for 2.3.1.157 extracted from

  • Craggs, P.D.; Mouilleron, S.; Rejzek, M.; de Chiara, C.; Young, R.J.; Field, R.A.; Argyrou, A.; de Carvalho, L.P.S.
    The Mechanism of acetyl transfer catalyzed by Mycobacterium tuberculosis GlmU (2018), Biochemistry, 57, 3387-3401 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.157

Crystallization (Commentary)

Crystallization (Comment) Organism
apo GlmU is crystallized at 20 °C using the sitting-drop vapor diffusion methodcrystal structure of a mimic of the Michaelis complex, with glucose 1-phosphate and acetyl-coenzyme A, helps us to propose the residues involved in deprotonation of glucosamine 1-phosphate and the loop movement that likely generates the active site required for glucosamine 1-phosphate to bind Mycobacterium tuberculosis
apo GlmU is crystallized at 20 °C using the sitting-drop vapor diffusion methodcrystal structure of a mimic of the Michaelis complex, with glucose 1-phosphate and acetyl-coenzyme A, indicates the residues involved in deprotonation of glucosamine 1-phosphate and the loop movement that likely generates the active site required for glucosamine 1-phosphate to bind Mycobacterium tuberculosis
in complex with acetyl-CoA and glucose 1-phosphate Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
butanoyl-CoA
-
 Mycobacterium tuberculosis
CoA
-
 Mycobacterium tuberculosis
crotonyl-CoA
-
 Mycobacterium tuberculosis
D-galactosamine 1-phosphate
-
 Mycobacterium tuberculosis
D-glucosamine 6-phosphate
-
 Mycobacterium tuberculosis
D-glucose 1-phosphate
-
 Mycobacterium tuberculosis
ethyl-CoA
-
 Mycobacterium tuberculosis
isobutanoyl-CoA
-
 Mycobacterium tuberculosis
malonyl-CoA
-
 Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.016
-
 alpha-D-glucosamine 1-phosphate cosubstrate acetoacetyl-CoA, pH 7.5, 30°C Mycobacterium tuberculosis
0.016
-
 alpha-D-glucosamine 1-phosphate pH 7.5, 30°C, cosubstrate: acetoacetyl-CoA Mycobacterium tuberculosis
0.06
-
 propionyl-CoA pH 7.5, 30°C Mycobacterium tuberculosis
0.06
-
 n-propionyl-CoA pH 7.5, 30°C Mycobacterium tuberculosis
0.25
-
 acetyl-CoA pH 7.5, 30°C Mycobacterium tuberculosis
0.29
-
 alpha-D-glucosamine 1-phosphate pH 7.5, 30°C Mycobacterium tuberculosis
0.29
-
 alpha-D-glucosamine 1-phosphate cosubstrate acetyl-CoA, pH 7.5, 30°C Mycobacterium tuberculosis
0.98
-
 alpha-D-glucosamine 1-phosphate cosubstrate propionyl-CoA, pH 7.5, 30°C Mycobacterium tuberculosis
0.98
-
 alpha-D-glucosamine 1-phosphate pH 7.5, 30°C, cosubstrate: n-propionyl-CoA Mycobacterium tuberculosis
1.1
-
 succinyl-CoA pH 7.5, 30°C Mycobacterium tuberculosis
1.8
-
 acetoacetyl-CoA pH 7.5, 30°C Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates Mycobacterium tuberculosis
Mg2+ required Mycobacterium tuberculosis
Mn2+ activates 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
-
 ?
acetyl-CoA + alpha-D-glucosamine 1-phosphate Mycobacterium tuberculosis the enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
acetyl-CoA + alpha-D-glucosamine 1-phosphate Mycobacterium tuberculosis ATCC 25177
-
 CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
acetyl-CoA + alpha-D-glucosamine 1-phosphate Mycobacterium tuberculosis ATCC 25177 the enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis A5U161
-
-
Mycobacterium tuberculosis A5U161 bifunctional N-acetyltransferase/uridylyltransferase, catalyzes reactions of EC 2.3.1.157 and EC 2.7.7.23
-
Mycobacterium tuberculosis ATCC 25177 A5U161
-
-
Mycobacterium tuberculosis ATCC 25177 A5U161 bifunctional N-acetyltransferase/uridylyltransferase, catalyzes reactions of EC 2.3.1.157 and EC 2.7.7.23
-

Purification (Commentary)

Purification (Comment) Organism
-
 Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetoacetyl-CoA + alpha-D-glucosamine 1-phosphate
-
 Mycobacterium tuberculosis CoA + N-acetoacetyl-alpha-D-glucosamine 1-phosphate
-
 ?
acetoacetyl-CoA + alpha-D-glucosamine 1-phosphate
-
 Mycobacterium tuberculosis ATCC 25177 CoA + N-acetoacetyl-alpha-D-glucosamine 1-phosphate
-
 ?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
-
 Mycobacterium tuberculosis CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
acetyl-CoA + alpha-D-glucosamine 1-phosphate the enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan Mycobacterium tuberculosis CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
acetyl-CoA + alpha-D-glucosamine 1-phosphate the enzyme utilizes ternary complex formation to transfer an acetyl from acetyl-coenzyme A to glucosamine 1-phosphate to form N-acetylglucosamine 1-phosphate. Steady-state kinetic studies and equilibrium binding experiments indicate that GlmU follows a steady-state ordered kinetic mechanism, with acetyl-coenzyme A binding first, which triggers a conformational change in GlmU, followed by glucosamine 1-phosphate binding. Coenzyme A is the last product to dissociate Mycobacterium tuberculosis CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
acetyl-CoA + alpha-D-glucosamine 1-phosphate
-
 Mycobacterium tuberculosis ATCC 25177 CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
acetyl-CoA + alpha-D-glucosamine 1-phosphate the enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan Mycobacterium tuberculosis ATCC 25177 CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
acetyl-CoA + alpha-D-glucosamine 1-phosphate the enzyme utilizes ternary complex formation to transfer an acetyl from acetyl-coenzyme A to glucosamine 1-phosphate to form N-acetylglucosamine 1-phosphate. Steady-state kinetic studies and equilibrium binding experiments indicate that GlmU follows a steady-state ordered kinetic mechanism, with acetyl-coenzyme A binding first, which triggers a conformational change in GlmU, followed by glucosamine 1-phosphate binding. Coenzyme A is the last product to dissociate Mycobacterium tuberculosis ATCC 25177 CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 ?
additional information GlmU follows a steady-state ordered kinetic mechanism, with acetyl-coenzyme A binding first, which triggers a conformational change in GlmU, followed by glucosamine 1-phosphate binding. Coenzyme A is the last product to dissociate Mycobacterium tuberculosis ?
-
-
additional information GlmU follows a steady-state ordered kinetic mechanism, with acetyl-coenzyme A binding first, which triggers a conformational change in GlmU, followed by glucosamine 1-phosphate binding. Coenzyme A is the last product to dissociate Mycobacterium tuberculosis ATCC 25177 ?
-
-
n-propionyl-CoA + alpha-D-glucosamine 1-phosphate
-
 Mycobacterium tuberculosis CoA + N-propionyl-alpha-D-glucosamine 1-phosphate
-
 ?
propionyl-CoA + alpha-D-glucosamine 1-phosphate
-
 Mycobacterium tuberculosis CoA + N-propionyl-alpha-D-glucosamine 1-phosphate
-
 ?
succinyl-CoA + alpha-D-glucosamine 1-phosphate
-
 Mycobacterium tuberculosis CoA + N-succinyl-alpha-D-glucosamine 1-phosphate
-
 ?

Synonyms

Synonyms Comment Organism
bifunctional N-acetyltransferase/uridylyltransferase
-
 Mycobacterium tuberculosis
GlmU
-
 Mycobacterium tuberculosis
GlmU bifunctional enzyme, also to possess the activity of EC 2.3.1.23, glucosamine-1-phosphate N-acetyltransferase Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Mycobacterium tuberculosis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.13
-
 alpha-D-glucosamine 1-phosphate cosubstrate acetoacetyl-CoA, pH 7.5, 30°C Mycobacterium tuberculosis
0.13
-
 alpha-D-glucosamine 1-phosphate pH 7.5, 30°C, cosubstrate: acetoacetyl-CoA Mycobacterium tuberculosis
0.5
-
 acetoacetyl-CoA pH 7.5, 30°C Mycobacterium tuberculosis
0.5
-
 propionyl-CoA pH 7.5, 30°C Mycobacterium tuberculosis
0.5
-
 n-propionyl-CoA pH 7.5, 30°C Mycobacterium tuberculosis
0.5
-
 alpha-D-glucosamine 1-phosphate cosubstrate propionyl-CoA, pH 7.5, 30°C Mycobacterium tuberculosis
0.5
-
 alpha-D-glucosamine 1-phosphate pH 7.5, 30°C, cosubstrate: n-propionyl-CoA Mycobacterium tuberculosis
0.9
-
 succinyl-CoA pH 7.5, 30°C Mycobacterium tuberculosis
2 8 acetyl-CoA pH 7.5, 30°C Mycobacterium tuberculosis
2 8 alpha-D-glucosamine 1-phosphate pH 7.5, 30°C Mycobacterium tuberculosis
2 8 alpha-D-glucosamine 1-phosphate cosubstrate acetyl-CoA, pH 7.5, 30°C Mycobacterium tuberculosis
2 8 alpha-D-glucosamine 1-phosphate pH 7.5, 30°C, cosubstrate: acetyl-CoA Mycobacterium tuberculosis

pH Optimum

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

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.3
-
 pH 7.5, 30°C Mycobacterium tuberculosis CoA
1
-
 pH 7.5, 30°C Mycobacterium tuberculosis crotonyl-CoA
1
-
 pH 7.5, 30°C Mycobacterium tuberculosis butanoyl-CoA
2
-
 pH 7.5, 30°C Mycobacterium tuberculosis malonyl-CoA
2
-
 pH 7.5, 30°C Mycobacterium tuberculosis isobutanoyl-CoA
5
-
 pH 7.5, 30°C Mycobacterium tuberculosis D-glucose 1-phosphate
10
-
 pH 7.5, 30°C Mycobacterium tuberculosis D-glucosamine 6-phosphate
120
-
 pH 7.5, 30°C Mycobacterium tuberculosis D-galactosamine 1-phosphate

General Information

General Information Comment Organism
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 Mycobacterium tuberculosis
metabolism the enzyme is responsible for the final two steps of the synthesis of UDP-N-acetylglucosamine, which is an essential precursor of peptidoglycan Mycobacterium tuberculosis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.28
-
 acetoacetyl-CoA pH 7.5, 30°C Mycobacterium tuberculosis
0.51
-
 alpha-D-glucosamine 1-phosphate cosubstrate propionyl-CoA, pH 7.5, 30°C Mycobacterium tuberculosis
0.51
-
 alpha-D-glucosamine 1-phosphate pH 7.5, 30°C, cosubstrate: n-propionyl-CoA Mycobacterium tuberculosis
0.82
-
 succinyl-CoA pH 7.5, 30°C Mycobacterium tuberculosis
8.1
-
 alpha-D-glucosamine 1-phosphate cosubstrate acetoacetyl-CoA, pH 7.5, 30°C Mycobacterium tuberculosis
8.1
-
 alpha-D-glucosamine 1-phosphate pH 7.5, 30°C, cosubstrate: acetoacetyl-CoA Mycobacterium tuberculosis
8.3
-
 propionyl-CoA pH 7.5, 30°C Mycobacterium tuberculosis
8.3
-
 n-propionyl-CoA pH 7.5, 30°C Mycobacterium tuberculosis
97
-
 alpha-D-glucosamine 1-phosphate pH 7.5, 30°C Mycobacterium tuberculosis
97
-
 alpha-D-glucosamine 1-phosphate cosubstrate acetyl-CoA, pH 7.5, 30°C Mycobacterium tuberculosis
110
-
 acetyl-CoA pH 7.5, 30°C Mycobacterium tuberculosis
112
-
 acetyl-CoA pH 7.5, 30°C Mycobacterium tuberculosis