Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli strain BL21 | Escherichia coli |
expression in Escherichia coli strain BL21 | Lacticaseibacillus casei |
Crystallization (Comment) | Organism |
---|---|
microseeding, E143A mutant | Lacticaseibacillus casei |
Protein Variants | Comment | Organism |
---|---|---|
E143A | almost inactive | Lacticaseibacillus casei |
E143D | almost inactive | Lacticaseibacillus casei |
E143Q | almost inactive | Lacticaseibacillus casei |
E146Q | completely inactive, no ATP binding is observed with this mutant | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
5,6,7,8-tetrahydrofolyl-Glu2 | 60% inhibition of ATP binding at 0.1 mM | Escherichia coli | |
Dihydropteroic acid | 5% inhibition of ATP binding at 0.1 mM | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.07 | - |
ATP | pH 9.75, temperature conditions not mentioned | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Escherichia coli | the enzyme catalyzes the MgATP-dependent ligation of L-glutamate to tetrahydrofolate coenzymes or to antifolates at the gamma-carboxyl of the terminal glutamate to form polyglutamate derivatives | ? | - |
? | |
additional information | Lacticaseibacillus casei | the enzyme catalyzes the MgATP-dependent ligation of L-glutamate to tetrahydrofolate coenzymes or to antifolates at the gamma-carboxyl of the terminal glutamate to form polyglutamate derivatives | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Lacticaseibacillus casei | - |
- |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.0003 | - |
mutant E143A, pH 9.75 | Lacticaseibacillus casei |
0.0005 | - |
mutant E143Q, pH 9.75 | Lacticaseibacillus casei |
0.00055 | - |
mutant E143D, pH 9.75 | Lacticaseibacillus casei |
0.2 | - |
wild type enzyme, pH 9.75 | Escherichia coli |
0.2 | - |
wild type enzyme, pH 9.75 | Lacticaseibacillus casei |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 5,10-methylene-5,6,7,8-tetrahydrofolate-Glu2 + L-glutamate | - |
Escherichia coli | ADP + phosphate + 5,10-methylene-5,6,7,8-tetrahydrofolyl-Glu3 | - |
? | |
ATP + 5,10-methylene-tetrahydrofolate-Glu2 + L-glutamate | - |
Lacticaseibacillus casei | ADP + phosphate + 5,10-methylene-tetrahydrofolyl-Glu3 | - |
? | |
ATP + 5,6,7,8-tetrahydrofolate-Glu2 + L-glutamate | - |
Escherichia coli | ADP + phosphate + 5,6,7,8-tetrahydrofolyl-Glu3 | - |
? | |
ATP + dihydropteroic acid + L-glutamate | enhancement of ATP binding is observed in the presence of this substrate. The substrate causes a conformational change in the inactive fraction of the enzyme which allows it to bind ATP | Escherichia coli | ADP + dihydropteroyl-Glu | - |
? | |
additional information | the enzyme catalyzes the MgATP-dependent ligation of L-glutamate to tetrahydrofolate coenzymes or to antifolates at the gamma-carboxyl of the terminal glutamate to form polyglutamate derivatives | Escherichia coli | ? | - |
? | |
additional information | the enzyme catalyzes the MgATP-dependent ligation of L-glutamate to tetrahydrofolate coenzymes or to antifolates at the gamma-carboxyl of the terminal glutamate to form polyglutamate derivatives | Lacticaseibacillus casei | ? | - |
? |