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2.3.1.6: choline O-acetyltransferase

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

Word Map on EC 2.3.1.6

Reaction

acetyl-CoA
+
choline
=
CoA
 +
O-acetylcholine

Synonyms

acetyl CoA:choline-O-acetyltransferase, acetyl-CoA:choline-O-acetyltransferase, acetyltransferase, choline, cChAT, chAcT, ChAT, choline acetyl transferase, choline acetylase, choline acetyltransferase, choline-acetyltransferase, pChAT, peripheral type of choline acetyltransferase

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.6 choline O-acetyltransferase

Engineering

Engineering on EC 2.3.1.6 - choline O-acetyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S102R
mutation in the catalytic domain and in the vicinity of the active site of the enzyme. The change affects protein structure and has a direct impact on the catalytic domain of the protein which abolishes embryo motility almost completely. Mutant fish display reduced embryonic motility from 24 hours post-fertilization onwards. The heart beats at normal rate at 48 hours post-fertilization but decreases over time and ceases around 5 days post-fertilization, resulting in death. The swim bladder fails to inflate. Heterozygotes do not exhibit any mobility or other obvious defects and become healthy adults
H268L
-
an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426
H268N
-
an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426
H393L
-
an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426
H393N
-
an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426
H426L
-
an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426
H426N
-
an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426
A513T
mutant associated with congenital myasthenic syndrome, shows enhanced interaction with heat shock proteins HSC/HSP70 and HSP90 and increased sensitivity to heat shock protein inhibition
P17A/P19A
mutant shows enhanced interaction with heat shock proteins HSC/HSP70 and HSP90 and increased sensitivity to heat shock protein inhibition
S440A
-
the wild-type enzyme is distributed predominantly in cytoplasm (88%), with the remainder (12%) bound to cellular membranes, mutation S440A results in localization of the enzyme entirely in cytoplasm
V18M
mutant associated with congenital myasthenic syndrome, shows enhanced interaction with heat shock proteins HSC/HSP70 and HSP90 and increased sensitivity to heat shock protein inhibition
N514R
-
is described as ChAT-R, the introduction of an Arg at position 514 in rat enzyme is predicted to provide the ionic charge required to interact with, and neutralize, the carboxyl group of carnitine
R452A
-
kinetic as well chemical modification studies have implicated the presence of an active site arginine in enzyme, whose function is to stabilize coenzyme binding, conserved arginines are converted to identify these residues
R453A
-
kinetic as well chemical modification studies have implicated the presence of an active site arginine in enzyme, whose function is to stabilize coenzyme binding, conserved arginines are converted to identify these residues
R458A
-
kinetic as well chemical modification studies have implicated the presence of an active site arginine in enzyme, whose function is to stabilize coenzyme binding, conserved arginines are converted to identify these residues
R463A
-
kinetic as well chemical modification studies have implicated the presence of an active site arginine in enzyme, whose function is to stabilize coenzyme binding, conserved arginines are converted to identify these residues
V459T/D460E/N461T
-
is described as ChAT-TET