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Literature summary for 2.3.3.13 extracted from

  • Casey, A.K.; Baugh, J.; Frantom, P.A.
    The slow-onset nature of allosteric inhibition in alpha-isopropylmalate synthase from Mycobacterium tuberculosis is mediated by a flexible loop (2012), Biochemistry, 51, 4773-4775.
    View publication on PubMed
Search for more literature for 2.3.3.13

Protein Variants

Protein Variants Comment Organism
D563A the enzyme is more sensitive to L-leucine inhibition compared to the wild type enzyme Mycobacterium tuberculosis
D563N the enzyme is more sensitive to L-leucine inhibition compared to the wild type enzyme Mycobacterium tuberculosis
D564A the enzyme is less sensitive to L-leucine inhibition compared to the wild type enzyme Mycobacterium tuberculosis
H540A the enzyme is less sensitive to L-leucine inhibition compared to the wild type enzyme Mycobacterium tuberculosis
M559A the enzyme is less sensitive to L-leucine inhibition compared to the wild type enzyme Mycobacterium tuberculosis
Q566A the enzyme is more sensitive to L-leucine inhibition compared to the wild type enzyme Mycobacterium tuberculosis
S560A inactive Mycobacterium tuberculosis
S560W the mutation does not affect the activity of the enzyme, but the enzyme is less sensitive to L-leucine inhibition compared to the wild type enzyme Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
L-isoleucine
-
 Mycobacterium tuberculosis
L-leucine slow-onset, allosteric inhibition by L-leucine Mycobacterium tuberculosis
L-methionine
-
 Mycobacterium tuberculosis
L-norleucine micromolar inhibitor Mycobacterium tuberculosis
L-norvaline micromolar inhibitor Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the enzyme requires a divalent metal for activity and is activated by monovalent cations Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxo-3-methylbutanoate + acetyl-CoA + H2O
-
 Mycobacterium tuberculosis 3-hydroxy-4-methyl-3-carboxypentanoate + CoA
-
 ?

Subunits

Subunits Comment Organism
dimer
-
 Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
alpha-isopropylmalate synthase I
-
 Mycobacterium tuberculosis
IPMS
-
 Mycobacterium tuberculosis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0023
-
 L-leucine mutant enzyme D563N, pH and temperature not specified in the publication Mycobacterium tuberculosis
0.003
-
 L-leucine mutant enzyme D563A, pH and temperature not specified in the publication Mycobacterium tuberculosis
0.0077
-
 L-leucine mutant enzyme Q566A, pH and temperature not specified in the publication Mycobacterium tuberculosis
0.012
-
 L-leucine wild type enzyme, pH and temperature not specified in the publication Mycobacterium tuberculosis
0.023
-
 L-leucine mutant enzyme H540A, pH and temperature not specified in the publication Mycobacterium tuberculosis
0.024
-
 L-leucine mutant enzyme D564A, pH and temperature not specified in the publication Mycobacterium tuberculosis
0.051
-
 L-leucine mutant enzyme S560W, pH and temperature not specified in the publication Mycobacterium tuberculosis
0.155
-
 L-leucine mutant enzyme M559A, pH and temperature not specified in the publication Mycobacterium tuberculosis