KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | MtIlvE displays a ping-pong kinetic mechanism. Analysis of steady-state and pre-steady-state kinetic isotope effects. Michaelis-Menten kinetics | Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-isoleucine + 2-oxoglutarate | Mycobacterium tuberculosis | - |
3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | Mycobacterium tuberculosis H37Rv | - |
3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | Mycobacterium tuberculosis ATCC 25618 | - |
3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | Mycobacterium tuberculosis | - |
4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | Mycobacterium tuberculosis H37Rv | - |
4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | Mycobacterium tuberculosis ATCC 25618 | - |
4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | Mycobacterium tuberculosis | - |
3-methyl-2-oxobutanoate + L-glutamate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WQ75 | - |
- |
Mycobacterium tuberculosis ATCC 25618 | P9WQ75 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WQ75 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate | MtIlvE displays a ping-pong kinetic mechanism. The phosphate ester of the PLP cofactor, and the alpha-amino group from L-glutamate and the active site Lys204, play roles in acid-base catalysis and binding, respectively. An intrinsic primary kinetic isotope effect is identified for the alpha-C-H bond cleavage of L-glutamate. Large solvent kinetic isotope effect values for the ping and pong half-reactions are also identified | Mycobacterium tuberculosis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamate + 2-oxoglutarate | - |
Mycobacterium tuberculosis | 2-oxoglutarate + L-glutamate | - |
r | |
L-glutamate + 2-oxoglutarate | - |
Mycobacterium tuberculosis H37Rv | 2-oxoglutarate + L-glutamate | - |
r | |
L-glutamate + 2-oxoglutarate | - |
Mycobacterium tuberculosis ATCC 25618 | 2-oxoglutarate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | - |
Mycobacterium tuberculosis | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | - |
Mycobacterium tuberculosis H37Rv | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-isoleucine + 2-oxoglutarate | - |
Mycobacterium tuberculosis ATCC 25618 | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | - |
Mycobacterium tuberculosis | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | - |
Mycobacterium tuberculosis H37Rv | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-leucine + 2-oxoglutarate | - |
Mycobacterium tuberculosis ATCC 25618 | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Mycobacterium tuberculosis | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Mycobacterium tuberculosis H37Rv | phenylpyruvate + L-glutamate | - |
r | |
L-phenylalanine + 2-oxoglutarate | - |
Mycobacterium tuberculosis ATCC 25618 | phenylpyruvate + L-glutamate | - |
r | |
L-valine + 2-oxoglutarate | - |
Mycobacterium tuberculosis | 3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
additional information | a broad substrate specificity is displayed by MtIlvE. But the enzyme is extremely specific for L-glutamate as the amino donor in the direction of branched-chain amino acid synthesis, and L-aspartate has no activity with the enzyme. 2-Oxo-phenylpyruvate is a 20fold poorer substrate, as is 2-oxo-3-methylthiobutyrate, which exhibits a very high Km value but a very robust V value, equivalent to those of the best branched-chain 2-oxo acid substrates | Mycobacterium tuberculosis | ? | - |
- |
|
additional information | a broad substrate specificity is displayed by MtIlvE. But the enzyme is extremely specific for L-glutamate as the amino donor in the direction of branched-chain amino acid synthesis, and L-aspartate has no activity with the enzyme. 2-Oxo-phenylpyruvate is a 20fold poorer substrate, as is 2-oxo-3-methylthiobutyrate, which exhibits a very high Km value but a very robust V value, equivalent to those of the best branched-chain 2-oxo acid substrates | Mycobacterium tuberculosis H37Rv | ? | - |
- |
|
additional information | a broad substrate specificity is displayed by MtIlvE. But the enzyme is extremely specific for L-glutamate as the amino donor in the direction of branched-chain amino acid synthesis, and L-aspartate has no activity with the enzyme. 2-Oxo-phenylpyruvate is a 20fold poorer substrate, as is 2-oxo-3-methylthiobutyrate, which exhibits a very high Km value but a very robust V value, equivalent to those of the best branched-chain 2-oxo acid substrates | Mycobacterium tuberculosis ATCC 25618 | ? | - |
- |
Subunits | Comment | Organism |
---|---|---|
homodimer | 2 * 40000, SDS-PAGE | Mycobacterium tuberculosis |
More | the three-dimensional structure reveals that each monomer is tethered by a substrate specificity loop to its partner molecule | Mycobacterium tuberculosis |
Synonyms | Comment | Organism |
---|---|---|
BcaT | - |
Mycobacterium tuberculosis |
branched-chain amino acid aminotransferase | - |
Mycobacterium tuberculosis |
IlvE | - |
Mycobacterium tuberculosis |
MtIlvE | - |
Mycobacterium tuberculosis |
Rv2210c | - |
Mycobacterium tuberculosis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Mycobacterium tuberculosis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Mycobacterium tuberculosis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | PLP, dependent on | Mycobacterium tuberculosis |
General Information | Comment | Organism |
---|---|---|
metabolism | the biosynthetic pathway of the branched-chain amino acids is essential for Mycobacterium tuberculosis growth and survival. The pyridoxal 5'-phosphate (PLP)-dependent branched-chain aminotransferase, IlvE. This enzyme is responsible for the final step of the synthesis of the branched-chain amino acids isoleucine, leucine, and valine. Enzyme MtIlvE is involved in the last step of the methionine salvage pathway, where it catalyzes the transfer of an amino group from any of the BCAAs to 2-oxo-3-methylthiobutyrate | Mycobacterium tuberculosis |