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Literature summary for 6.2.1.9 extracted from

  • Elwell,M.; Hersh, L.B.
    Substrate-dependent dissociation of malate thiokinase (1979), J. Biol. Chem., 254, 2434-2438.
    View publication on PubMed
Search for more literature for 6.2.1.9

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34000
-
 2 * 34000 (alpha) + 2 * 42500 (beta), SDS-PAGE, the phosphoenzyme has an alpha2beta2 structure Pseudomonas sp.
42500
-
 2 * 34000 (alpha) + 2 * 42500 (beta), SDS-PAGE, the phosphoenzyme has an alpha2beta2 structure Pseudomonas sp.
255000
-
 gel filtration, nonphosphorylated enzyme, in presence of 20% sucrose Pseudomonas sp.
300000
-
 gel filtration, nonphosphorylated enzyme, in absence of sucrose Pseudomonas sp.

Organism

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

Purification (Commentary)

Purification (Comment) Organism
-
 Pseudomonas sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
7.4
-
-
 Pseudomonas sp.

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
-
 ?

Subunits

Subunits Comment Organism
tetramer 2 * 34000 (alpha) + 2 * 42500 (beta), SDS-PAGE, the phosphoenzyme has an alpha2beta2 structure Pseudomonas sp.

pH Stability

pH Stability pH Stability Maximum Comment Organism
additional information
-
 the phosphorylated enzyme is acid labile and base stable Pseudomonas sp.