Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Frantom, P.A.
    Structural and functional characterization of alpha-isopropylmalate synthase and citramalate synthase, members of the LeuA dimer superfamily (2012), Arch. Biochem. Biophys., 519, 202-209.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.3.3.13 D546A the enzyme shows wild type activity but is not inhibited by L-leucine Mycobacterium tuberculosis
2.3.3.13 D563N the enzyme shows wild type activity but is not inhibited by L-leucine Mycobacterium tuberculosis
2.3.3.13 Y410F the mutant is insensitive to L-leucine inhibition despite retaining significant binding affinity for the molecule Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.3.13 L-isoleucine noncompetitive inhibitor Mycobacterium tuberculosis
2.3.3.13 L-leucine noncompetitive inhibitor versus 2-oxo-3-methylbutanoate Mycobacterium tuberculosis
2.3.3.13 L-norleucine noncompetitive inhibitor Mycobacterium tuberculosis
2.3.3.13 L-norvaline noncompetitive inhibitor Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.3.13 Co2+ Co2+ is capable of supporting robust catalytic activity Mycobacterium tuberculosis
2.3.3.13 K+ K+ is the kinetically preferred ion Mycobacterium tuberculosis
2.3.3.13 Mg2+ Mg2+ is capable of supporting robust catalytic activity Mycobacterium tuberculosis
2.3.3.13 Mn2+ Mn2+ is capable of supporting robust catalytic activity Mycobacterium tuberculosis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.3.13 144000
-
-
Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
2.3.3.13 Mycobacterium tuberculosis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.3.13 2-oxo-3-methylbutanoate + acetyl-CoA + H2O the enzyme catalyzes a Claisen-condensation between acetyl-CoA and 2-oxo-3-methylbutanoate (alpha-ketoisovalerate) followed by hydrolysis to form 3-hydroxy-4-methyl-3-carboxypentanoate (alpha-isopropylmalate) and CoA Mycobacterium tuberculosis 3-hydroxy-4-methyl-3-carboxypentanoate + CoA
-
?

Subunits

EC Number Subunits Comment Organism
2.3.3.13 homodimer
-
Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
2.3.3.13 alpha-isopropylmalate synthase I
-
Mycobacterium tuberculosis
2.3.3.13 IPMS
-
Mycobacterium tuberculosis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.3.3.13 0.017
-
L-leucine pH and temperature not specified in the publication Mycobacterium tuberculosis