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2.3.1.7: carnitine O-acetyltransferase

This is an abbreviated version!
For detailed information about carnitine O-acetyltransferase, go to the full flat file.

Word Map on EC 2.3.1.7

Reaction

acetyl-CoA
+
carnitine
=
CoA
 +
O-acetylcarnitine

Synonyms

acetyl-CoA-carnitine O-acetyltransferase, acetylcarnitine transferase, acuJ, CarAc, CARAT, carnitine acetyl coenzyme A transferase, carnitine acetyl transferase, carnitine acetylase, carnitine acetyltransferase, carnitine acetyltransferase CAT2, carnitine acetyltransferase Cat2p, carnitine acetyltransferase Yat1p, carnitine acetyltransferase Yat2p, carnitine-acetyl-CoA transferase, CAT, CAT2, CATC, CRAT, CT-CAT, CTN1, CTN2, CTN3, H-CAT, P-CAT, S-CAT1, S-CAT2, Yat1

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.7 carnitine O-acetyltransferase

Engineering

Engineering on EC 2.3.1.7 - carnitine O-acetyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F545A
increases Km for both substrates
F545Y
minor effects on Km for both substrates
R497Q
increases Km for both substrates
T444A
increases Km for both substrates
V569M
missense variant idientified in a patient affected by Leigh syndrome. Proband-derived fibroblasts show carnitine acetyltransferase deficiency. The mutation severely impairs catalytic function toward acetyl-CoA, and also toward propionyl-CoA and octanoyl-CoA, reducing the Vmax of acetyl-CoA, propionyl-CoA, and octanoyl-CoA to 24%, 29%, and 27%, respectively, of wild-type
Y110C
missense variant idientified in a patient affected by Leigh syndrome. Proband-derived fibroblasts show carnitine acetyltransferase deficiency. The mutation severely impairs catalytic function toward acetyl-CoA, reducing the Vmax toward acetyl-CoA, propionyl-CoA, and octanoyl-CoA to 32%, 45%, and 61% of wild-type
Y431A
increases Km for both substrates
Y431F
increases Km for both substrates
F565A
-
used for crystallization, only minor effect on protein structure, increased activity with acetyl-CoA
H343A
mutant enzymje shows no activity with acetyl-CoA and hexanoyl-CoA
H343E
kcat/KM for acetyl-CoA is 9.8fold lower than wild-type value, mutant enzyme shows mo activity with hexanoyl-CoA as substrate
M564A
-
used for crystallization, decreased activity with acetyl-CoA and butyryl-CoA
M564G
S554A
kcat/KM for acetyl-CoA is 109fold lower than wild-type value, kcat/Km for hexanoyl-CoA is 8fold lower than wild-type value
S554A/M564G
kcat/KM for acetyl-CoA is 196fold lower than wild-type value, kcat/Km for hexanoyl-CoA is 4fold lower than wild-type value
D356A/M564G
-
shows 6fold higher activity toward palmitoyl-CoA than that of the single mutant M564G and a new activity toward stearoyl-CoA. Mutations convert the enzyme into a pseudo carnitine palmitoyltransferase in terms of substrate specificity
E347A
complete loss of activity
H343A
complete loss of activity
M564A
lowered activity with acetyl-CoA, increased activity with longer chain acyl-CoAs
M564G
T465V/T467N/R518N
-
3fold improved catalytic efficiency toward choline (Kcat/Km) compared with that of the wild-type enzyme