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Literature summary for 4.1.3.24 extracted from

  • Hersh, L.B.
    Malate adenosine triphosphate lyase. Separation of the reaction into a malate thiokinase and malyl coenzyme A lyase (1973), J. Biol. Chem., 248, 7295-7303.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.035
-
acetyl-CoA
-
Pseudomonas sp.
0.1
-
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
-
Pseudomonas sp.
0.8
-
glyoxylate
-
Pseudomonas sp.

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
Shaw strain 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
0.47
-
-
Pseudomonas sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
-
Pseudomonas sp. acetyl-CoA + glyoxylate
-
r
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
-
Pseudomonas sp. MA acetyl-CoA + glyoxylate
-
r
acetyl-CoA + glyoxylate
-
Pseudomonas sp. (3S)-3-carboxy-3-hydroxypropanoyl-CoA
-
r