EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.3.1.157 | 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 |
2.3.1.157 | 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 |
2.3.1.157 | in complex with acetyl-CoA and glucose 1-phosphate | Mycobacterium tuberculosis |
2.7.7.23 | 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 |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.157 | butanoyl-CoA | - |
Mycobacterium tuberculosis | |
2.3.1.157 | CoA | - |
Mycobacterium tuberculosis | |
2.3.1.157 | crotonyl-CoA | - |
Mycobacterium tuberculosis | |
2.3.1.157 | D-galactosamine 1-phosphate | - |
Mycobacterium tuberculosis | |
2.3.1.157 | D-glucosamine 6-phosphate | - |
Mycobacterium tuberculosis | |
2.3.1.157 | D-glucose 1-phosphate | - |
Mycobacterium tuberculosis | |
2.3.1.157 | ethyl-CoA | - |
Mycobacterium tuberculosis | |
2.3.1.157 | isobutanoyl-CoA | - |
Mycobacterium tuberculosis | |
2.3.1.157 | malonyl-CoA | - |
Mycobacterium tuberculosis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.157 | 0.016 | - |
alpha-D-glucosamine 1-phosphate | cosubstrate acetoacetyl-CoA, pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 0.016 | - |
alpha-D-glucosamine 1-phosphate | pH 7.5, 30°C, cosubstrate: acetoacetyl-CoA | Mycobacterium tuberculosis | |
2.3.1.157 | 0.06 | - |
propionyl-CoA | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 0.06 | - |
n-propionyl-CoA | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 0.25 | - |
acetyl-CoA | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 0.29 | - |
alpha-D-glucosamine 1-phosphate | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 0.29 | - |
alpha-D-glucosamine 1-phosphate | cosubstrate acetyl-CoA, pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 0.98 | - |
alpha-D-glucosamine 1-phosphate | cosubstrate propionyl-CoA, pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 0.98 | - |
alpha-D-glucosamine 1-phosphate | pH 7.5, 30°C, cosubstrate: n-propionyl-CoA | Mycobacterium tuberculosis | |
2.3.1.157 | 1.1 | - |
succinyl-CoA | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 1.8 | - |
acetoacetyl-CoA | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.7.7.23 | 0.008 | - |
UTP | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.7.7.23 | 0.03 | - |
N-acetyl-alpha-D-glucosamine 1-phosphate | pH 7.5, 30°C | Mycobacterium tuberculosis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.157 | Ca2+ | activates | Mycobacterium tuberculosis | |
2.3.1.157 | Mg2+ | required | Mycobacterium tuberculosis | |
2.3.1.157 | Mn2+ | activates | Mycobacterium tuberculosis | |
2.7.7.23 | Ca2+ | activates | Mycobacterium tuberculosis | |
2.7.7.23 | Mg2+ | required | Mycobacterium tuberculosis | |
2.7.7.23 | Mn2+ | activates | Mycobacterium tuberculosis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.157 | acetyl-CoA + alpha-D-glucosamine 1-phosphate | Mycobacterium tuberculosis | - |
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
2.3.1.157 | 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 | - |
? | |
2.3.1.157 | acetyl-CoA + alpha-D-glucosamine 1-phosphate | Mycobacterium tuberculosis ATCC 25177 | - |
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
2.3.1.157 | 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 | - |
? | |
2.7.7.23 | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | Mycobacterium tuberculosis | - |
diphosphate + UDP-N-acetyl-alpha-D-glucosamine | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.157 | Mycobacterium tuberculosis | A5U161 | - |
- |
2.3.1.157 | Mycobacterium tuberculosis | A5U161 | bifunctional N-acetyltransferase/uridylyltransferase, catalyzes reactions of EC 2.3.1.157 and EC 2.7.7.23 | - |
2.3.1.157 | Mycobacterium tuberculosis ATCC 25177 | A5U161 | - |
- |
2.3.1.157 | Mycobacterium tuberculosis ATCC 25177 | A5U161 | bifunctional N-acetyltransferase/uridylyltransferase, catalyzes reactions of EC 2.3.1.157 and EC 2.7.7.23 | - |
2.7.7.23 | Mycobacterium tuberculosis | A5U161 | - |
- |
2.7.7.23 | Mycobacterium tuberculosis ATCC 25177 | A5U161 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.3.1.157 | - |
Mycobacterium tuberculosis |
2.7.7.23 | - |
Mycobacterium tuberculosis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.157 | acetoacetyl-CoA + alpha-D-glucosamine 1-phosphate | - |
Mycobacterium tuberculosis | CoA + N-acetoacetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
2.3.1.157 | acetoacetyl-CoA + alpha-D-glucosamine 1-phosphate | - |
Mycobacterium tuberculosis ATCC 25177 | CoA + N-acetoacetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
2.3.1.157 | acetyl-CoA + alpha-D-glucosamine 1-phosphate | - |
Mycobacterium tuberculosis | CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
2.3.1.157 | 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 | - |
? | |
2.3.1.157 | 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 | - |
? | |
2.3.1.157 | acetyl-CoA + alpha-D-glucosamine 1-phosphate | - |
Mycobacterium tuberculosis ATCC 25177 | CoA + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
? | |
2.3.1.157 | 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 | - |
? | |
2.3.1.157 | 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 | - |
? | |
2.3.1.157 | 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 | ? | - |
- |
|
2.3.1.157 | 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 | ? | - |
- |
|
2.3.1.157 | n-propionyl-CoA + alpha-D-glucosamine 1-phosphate | - |
Mycobacterium tuberculosis | CoA + N-propionyl-alpha-D-glucosamine 1-phosphate | - |
? | |
2.3.1.157 | propionyl-CoA + alpha-D-glucosamine 1-phosphate | - |
Mycobacterium tuberculosis | CoA + N-propionyl-alpha-D-glucosamine 1-phosphate | - |
? | |
2.3.1.157 | succinyl-CoA + alpha-D-glucosamine 1-phosphate | - |
Mycobacterium tuberculosis | CoA + N-succinyl-alpha-D-glucosamine 1-phosphate | - |
? | |
2.7.7.23 | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate | - |
Mycobacterium tuberculosis | diphosphate + UDP-N-acetyl-alpha-D-glucosamine | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.1.157 | bifunctional N-acetyltransferase/uridylyltransferase | - |
Mycobacterium tuberculosis |
2.3.1.157 | GlmU | - |
Mycobacterium tuberculosis |
2.3.1.157 | GlmU | bifunctional enzyme, also to possess the activity of EC 2.3.1.23, glucosamine-1-phosphate N-acetyltransferase | Mycobacterium tuberculosis |
2.7.7.23 | bifunctional N-acetyltransferase/uridylyltransferase | - |
Mycobacterium tuberculosis |
2.7.7.23 | GlmU | bifunctional enzyme, also to possess the activity of EC 2.7.7.157, glucosamine-1-phosphate N-acetyltransferase | Mycobacterium tuberculosis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.1.157 | 30 | - |
assay at | Mycobacterium tuberculosis |
2.7.7.23 | 30 | - |
assay at | Mycobacterium tuberculosis |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.157 | 0.13 | - |
alpha-D-glucosamine 1-phosphate | cosubstrate acetoacetyl-CoA, pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 0.13 | - |
alpha-D-glucosamine 1-phosphate | pH 7.5, 30°C, cosubstrate: acetoacetyl-CoA | Mycobacterium tuberculosis | |
2.3.1.157 | 0.5 | - |
acetoacetyl-CoA | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 0.5 | - |
propionyl-CoA | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 0.5 | - |
n-propionyl-CoA | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 0.5 | - |
alpha-D-glucosamine 1-phosphate | cosubstrate propionyl-CoA, pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 0.5 | - |
alpha-D-glucosamine 1-phosphate | pH 7.5, 30°C, cosubstrate: n-propionyl-CoA | Mycobacterium tuberculosis | |
2.3.1.157 | 0.9 | - |
succinyl-CoA | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 2 | 8 | acetyl-CoA | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 2 | 8 | alpha-D-glucosamine 1-phosphate | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 2 | 8 | alpha-D-glucosamine 1-phosphate | cosubstrate acetyl-CoA, pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 2 | 8 | alpha-D-glucosamine 1-phosphate | pH 7.5, 30°C, cosubstrate: acetyl-CoA | Mycobacterium tuberculosis | |
2.7.7.23 | 100 | - |
N-acetyl-alpha-D-glucosamine 1-phosphate | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.7.7.23 | 120 | - |
UTP | pH 7.5, 30°C | Mycobacterium tuberculosis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.3.1.157 | 7.5 | - |
assay at | Mycobacterium tuberculosis |
2.7.7.23 | 7.5 | - |
assay at | Mycobacterium tuberculosis |
EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|---|
2.3.1.157 | 0.3 | - |
pH 7.5, 30°C | Mycobacterium tuberculosis | CoA | |
2.3.1.157 | 1 | - |
pH 7.5, 30°C | Mycobacterium tuberculosis | crotonyl-CoA | |
2.3.1.157 | 1 | - |
pH 7.5, 30°C | Mycobacterium tuberculosis | butanoyl-CoA | |
2.3.1.157 | 2 | - |
pH 7.5, 30°C | Mycobacterium tuberculosis | malonyl-CoA | |
2.3.1.157 | 2 | - |
pH 7.5, 30°C | Mycobacterium tuberculosis | isobutanoyl-CoA | |
2.3.1.157 | 5 | - |
pH 7.5, 30°C | Mycobacterium tuberculosis | D-glucose 1-phosphate | |
2.3.1.157 | 10 | - |
pH 7.5, 30°C | Mycobacterium tuberculosis | D-glucosamine 6-phosphate | |
2.3.1.157 | 120 | - |
pH 7.5, 30°C | Mycobacterium tuberculosis | D-galactosamine 1-phosphate |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.3.1.157 | 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 |
2.3.1.157 | 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 |
2.7.7.23 | 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 |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.157 | 0.28 | - |
acetoacetyl-CoA | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 0.51 | - |
alpha-D-glucosamine 1-phosphate | cosubstrate propionyl-CoA, pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 0.51 | - |
alpha-D-glucosamine 1-phosphate | pH 7.5, 30°C, cosubstrate: n-propionyl-CoA | Mycobacterium tuberculosis | |
2.3.1.157 | 0.82 | - |
succinyl-CoA | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 8.1 | - |
alpha-D-glucosamine 1-phosphate | cosubstrate acetoacetyl-CoA, pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 8.1 | - |
alpha-D-glucosamine 1-phosphate | pH 7.5, 30°C, cosubstrate: acetoacetyl-CoA | Mycobacterium tuberculosis | |
2.3.1.157 | 8.3 | - |
propionyl-CoA | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 8.3 | - |
n-propionyl-CoA | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 97 | - |
alpha-D-glucosamine 1-phosphate | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 97 | - |
alpha-D-glucosamine 1-phosphate | cosubstrate acetyl-CoA, pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 110 | - |
acetyl-CoA | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.3.1.157 | 112 | - |
acetyl-CoA | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.7.7.23 | 3333 | - |
N-acetyl-alpha-D-glucosamine 1-phosphate | pH 7.5, 30°C | Mycobacterium tuberculosis | |
2.7.7.23 | 15000 | - |
UTP | pH 7.5, 30°C | Mycobacterium tuberculosis |