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Literature summary for 6.2.1.9 extracted from

  • Hersh, L.B.
    Malate thiokinase. The reaction mechanism as determined by initial rate studies (1974), J. Biol. Chem., 249, 6264-6271.
    View publication on PubMed
Search for more literature for 6.2.1.9

Inhibitors

Inhibitors Comment Organism Structure
Chromium-ATP dead-end inhibitor Pseudomonas sp.
phosphate product inhibitor Pseudomonas sp.
succinyl-CoA product inhibitor Pseudomonas sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Pseudomonas sp.

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
-
-
Pseudomonas sp. MA
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + malate + CoA
-
 Pseudomonas sp. ADP + phosphate + malyl-CoA
-
 ?
ATP + malate + CoA
-
 Pseudomonas sp. MA ADP + phosphate + malyl-CoA
-
 ?
ATP + succinate + CoA random addition of substrates Pseudomonas sp. ADP + phosphate + succinyl-CoA
-
 ?
ATP + succinate + CoA random addition of substrates Pseudomonas sp. MA ADP + phosphate + succinyl-CoA
-
 ?
additional information arsenoslysis reaction is sequentially ordered, with succinyl-CoA binding prior to arsenate Pseudomonas sp. ?
-
 ?
additional information enzyme catalyzes a slow ATP-ADP exchange reaction which is stimulated by coenzyme A or succinyl-CoA, and a slow succinate-succinyl-CoA exchange reaction, which requires phosphate Pseudomonas sp. ?
-
 ?
additional information arsenolysis reaction Pseudomonas sp. ?
-
 ?
additional information arsenoslysis reaction is sequentially ordered, with succinyl-CoA binding prior to arsenate Pseudomonas sp. MA ?
-
 ?
additional information enzyme catalyzes a slow ATP-ADP exchange reaction which is stimulated by coenzyme A or succinyl-CoA, and a slow succinate-succinyl-CoA exchange reaction, which requires phosphate Pseudomonas sp. MA ?
-
 ?
additional information arsenolysis reaction Pseudomonas sp. MA ?
-
 ?