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Literature summary for 2.3.1.21 extracted from

  • Motlagh, L.; Golbik, R.; Sippl, W.; Zierz, S.
    Stabilization of the thermolabile variant S113L of carnitine palmitoyltransferase II (2016), Neurol. Genet., 2, e53 .
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
medicine problems in CPT2 deficiency originating from the S113L mutation might be at least partially related to an impaired thermal stability of the protein Homo sapiens

Protein Variants

Protein Variants Comment Organism
S113L mutant displays an abnormal thermal destabilization at 40°C and 45°C consistent with an increased flexibility at 40°C. Preincubation with L-carnitine and acyl-L-carnitines containing more than 10 carbons in the acyl side-chain stabilizes the mutant Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
palmitoyl-CoA thermally destabilizes bith wild-type and mutant S113L Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P23786
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
33
-
mutant S113L, pH 7.4, 30°C Homo sapiens
39
-
wild-type, pH 7.4, 30°C Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
palmitoyl-CoA + L-carnitine
-
Homo sapiens CoA + L-palmitoylcarnitine
-
?