EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.6.1.42 | purified recombinant enzyme MtIlvE bound by inhibitor D-cycloserine and pyridoxamine (PMP), X-ray diffraction structure determination and analysis at 1.7 A resolution | Mycobacterium tuberculosis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.6.1.42 | D-cycloserine | DCS, mechanism-based inhibition of the Mycobacterium tuberculosis branched-chain aminotransferase by D-cycloserine, mechanism and enzyme-bound three-dimensional structure with a role of residue C196, overview. Time and concentration-dependent inactivation. The structure of the covalent D-cycloserine-PMP adduct bound to MtIlvE reveals that the D-cycloserine ring is planar and aromatic | Mycobacterium tuberculosis | |
2.6.1.42 | L-Cycloserine | LCS, mechanism-based inhibition of the Mycobacterium tuberculosis branched-chain aminotransferase by L-cycloserine, mchanism overview, time and concentration-dependent inactivation | Mycobacterium tuberculosis | |
2.6.1.42 | additional information | L-cycloserine is a 10fold better inhibitor of Mycobacterium tuberculosis growth than D-cycloserine. Both the D-cycloserine and L-cycloserine-PMP complexes have the same mass, and are likely to be the same aromatized, isoxazole product, but the kinetics of formation of the MtIlvE D-cycloserine-PMP and MtIlvE L-cycloserine-PMP adducts are quite different. While the kinetics of the formation of the MtIlvE D-cycloserine-PMP complex can be fit to a single exponential, the formation of the MtIlvE L-cycloserine-PMP complex occurs in two steps. No inhibition of the enzyme by propargylglycine (an inhibitor of cystathionine gamma-synthase), by gabaculine (an inhibitor of GABA aminotransferase and ornithine decarboxylase) or by difluoromethylornithine (DFMO, the inhibitor of ornithine decarboxylase). Also gabapentin, a potent inhibitor of the cytosolic isozyme hBCATc, has no effect on the activity of MtIlvE | Mycobacterium tuberculosis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.6.1.42 | L-isoleucine + 2-oxoglutarate | Mycobacterium tuberculosis | - |
3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
2.6.1.42 | L-isoleucine + 2-oxoglutarate | Mycobacterium tuberculosis H37Rv | - |
3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
2.6.1.42 | L-leucine + 2-oxoglutarate | Mycobacterium tuberculosis | - |
4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
2.6.1.42 | L-leucine + 2-oxoglutarate | Mycobacterium tuberculosis H37Rv | - |
4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
2.6.1.42 | L-valine + 2-oxoglutarate | Mycobacterium tuberculosis | - |
3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
2.6.1.42 | L-valine + 2-oxoglutarate | Mycobacterium tuberculosis H37Rv | - |
3-methyl-2-oxobutanoate + L-glutamate | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.6.1.42 | Mycobacterium tuberculosis | P9WQ75 | - |
- |
2.6.1.42 | Mycobacterium tuberculosis H37Rv | P9WQ75 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.6.1.42 | L-isoleucine + 2-oxoglutarate | - |
Mycobacterium tuberculosis | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
2.6.1.42 | L-isoleucine + 2-oxoglutarate | - |
Mycobacterium tuberculosis H37Rv | 3-methyl-2-oxopentanoate + L-glutamate | - |
r | |
2.6.1.42 | L-leucine + 2-oxoglutarate | - |
Mycobacterium tuberculosis | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
2.6.1.42 | L-leucine + 2-oxoglutarate | - |
Mycobacterium tuberculosis H37Rv | 4-methyl-2-oxopentanoate + L-glutamate | - |
r | |
2.6.1.42 | L-valine + 2-oxoglutarate | - |
Mycobacterium tuberculosis | 3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
2.6.1.42 | L-valine + 2-oxoglutarate | - |
Mycobacterium tuberculosis H37Rv | 3-methyl-2-oxobutanoate + L-glutamate | - |
r | |
2.6.1.42 | additional information | MtIlvE is an L-amino acid aminotransferase | Mycobacterium tuberculosis | ? | - |
- |
|
2.6.1.42 | additional information | MtIlvE is an L-amino acid aminotransferase | Mycobacterium tuberculosis H37Rv | ? | - |
- |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.6.1.42 | homodimer | - |
Mycobacterium tuberculosis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.6.1.42 | BcaT | - |
Mycobacterium tuberculosis |
2.6.1.42 | branched-chain aminotransferase | - |
Mycobacterium tuberculosis |
2.6.1.42 | IlvE | - |
Mycobacterium tuberculosis |
2.6.1.42 | MtIlvE | - |
Mycobacterium tuberculosis |
2.6.1.42 | Rv2210c | locus name | Mycobacterium tuberculosis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.6.1.42 | 25 | - |
assay at | Mycobacterium tuberculosis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.6.1.42 | 8 | - |
assay at | Mycobacterium tuberculosis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.6.1.42 | pyridoxal 5'-phosphate | PLP, dependent on | Mycobacterium tuberculosis |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.6.1.42 | additional information | - |
additional information | inhibition kinetics of L- and D-cyclserine, the inactivation follows pseudo-first-order kinetics, at least one molar equivalent of inhibitor binds to one molecule of enzyme for inactivation. Rapid inactivation by L-cycloserine with the second-order rate constant of inactivation kinact/KI_LCS of 7.32 M/s being greater than kinact/KI_DCS of 0.12 M/s | Mycobacterium tuberculosis |
EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|---|
2.6.1.42 | 0.088 | - |
pH 8.0, 25°C, recombinant enzyme | Mycobacterium tuberculosis | L-Cycloserine |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.6.1.42 | physiological function | the branched-chain aminotransferase is a pyridoxal 5'-phosphate (PLP)-dependent enzyme responsible for the final step in the biosynthesis of all three branched-chain amino acids, L-leucine, L-isoleucine, and L-valine, in bacteria | Mycobacterium tuberculosis |