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Literature summary for 1.1.1.100 extracted from

  • Silva, R.G.; Rosado, L.A.; Santos, D.S.; Basso, L.A.
    Mycobacterium tuberculosis beta-ketoacyl-ACP reductase: alpha-secondary kinetic isotope effects and kinetic and equilibrium mechanisms of substrate binding (2008), Arch. Biochem. Biophys., 471, 1-10.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
isoform MabA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein, modified purification protocol Mycobacterium tuberculosis

Reaction

Reaction Comment Organism Reaction ID
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+ positive cooperativity in binding of NADPH to enzyme, no cooperativity in binding of acetoacyl-CoA. Pre-existing equilibrium of two forms of free MabA in solution followed by a bimolecular association process Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
increase in alpha-secondary deuterium kinetic isotope effect values measured at pH 10 as compared to those obtained at pH 7 points to isotope- and pH-sensitive steps occurring concomitantly Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
NADPH positive cooperativity in binding to enzyme Mycobacterium tuberculosis