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Literature summary for 2.6.1.42 extracted from

  • Amorim Franco, T.M.; Hegde, S.; Blanchard, J.S.
    Chemical mechanism of the branched-chain aminotransferase IlvE from Mycobacterium tuberculosis (2016), Biochemistry, 55, 6295-6303 .
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WQ75
-
-
Mycobacterium tuberculosis ATCC 25618 P9WQ75
-
-
Mycobacterium tuberculosis H37Rv P9WQ75
-
-

Reaction

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 and Products (Substrate)

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

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

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate PLP, dependent on Mycobacterium tuberculosis

General Information

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