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

BRENDA support

Literature summary for 2.3.3.13 extracted from

  • Casey, A.K.; Schwalm, E.L.; Hays, B.N.; Frantom, P.A.
    V-type allosteric inhibition is described by a shift in the rate-determining step for alpha-isopropylmalate synthase from Mycobacterium tuberculosis (2013), Biochemistry, 52, 6737-6739.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
Q84A the mutant exhibits kcat values similar to that of the L-leucine inhibited wild type enzyme Mycobacterium tuberculosis
Y410F the mutant exhibits kcat values similar to that of the L-leucine inhibited wild type enzyme Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
L-leucine the enzyme retains approximately 10% activity in the presence of saturating concentrations of L-leucine Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + 3-methyl-2-oxobutanoate + H2O Mycobacterium tuberculosis
-
(2S)-2-isopropylmalate + CoA
-
?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + 3-methyl-2-oxobutanoate + H2O
-
Mycobacterium tuberculosis (2S)-2-isopropylmalate + CoA
-
?

Synonyms

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