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Literature summary for 2.3.3.9 extracted from

  • Smith, C.V.; Huang, C.C.; Miczak, A.; Russell, D.G.; Sacchettini, J.C.; Honer zu Bentrup, K.
    Biochemical and structural studies of malate synthase from Mycobacterium tuberculosis (2003), J. Biol. Chem., 278, 1735-1743.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment) Organism
mixed alpha/beta structure Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
Bromopyruvate
-
Mycobacterium tuberculosis
glycolate only at fairly high concentration Mycobacterium tuberculosis
malate 1.0 mM, 50% inhibition Mycobacterium tuberculosis
additional information 3-phosphoglycerate, 6-phosphogluconate, malonic acid; not: fructose 1,6-bisphosphate Mycobacterium tuberculosis
oxalate
-
Mycobacterium tuberculosis
phosphoenolpyruvate
-
Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.03
-
acetyl-CoA recombinant enzyme Mycobacterium tuberculosis
0.057
-
glyoxylate recombinant enzyme Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ absolute requirement for divalent cation, maximal activity with 5 mM Mg2+ Mycobacterium tuberculosis
Mn2+ 40% of the activation with Mg2+ Mycobacterium tuberculosis
additional information Co2+, Fe2+, Ca2+, Ba2+, Ni2+, Cd2+, Zn2+, Cu2+, Hg2+ are not able to support the activity of enzyme Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Mycobacterium tuberculosis

Reaction

Reaction Comment Organism Reaction ID
acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA mechanism Mycobacterium tuberculosis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6
-
recombinant enzyme Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glyoxylate + acetyl-CoA + H2O structure of enzyme-substrate complex Mycobacterium tuberculosis (S)-malate + CoA
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Mycobacterium tuberculosis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.06
-
Bromopyruvate
-
Mycobacterium tuberculosis
0.2
-
phosphoenolpyruvate
-
Mycobacterium tuberculosis
0.4
-
oxalate
-
Mycobacterium tuberculosis
0.9
-
glycolate
-
Mycobacterium tuberculosis