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Information on EC 2.3.1.6 - choline O-acetyltransferase and Organism(s) Drosophila melanogaster and UniProt Accession P07668
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2.3.1.6 choline O-acetyltransferaseIUBMB Comments
Propanoyl-CoA can act, more slowly, in place of acetyl-CoA.
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Word Map
- 2.3.1.6
-
cholinergic
- acetylcholine
- nerve
- acetylcholinesterase
- hippocampus
- forebrain
-
neurotransmitter
-
innervation
- alzheimer
- cortical
- axon
-
medial
-
muscarinic
- striatum
-
neurochemical
- spinal
-
retrograde
-
maze
-
ventral
-
basalis
- ganglion
-
neurotrophic
- septal
- ngf
-
diagonal
-
gabaergic
- myenteric
-
interneurons
-
vacht
- motoneuron
-
chat-positive
-
afferent
- meynert
-
magnocellularis
-
presynaptic
-
varicosity
-
parasympathetic
-
non-cholinergic
-
preganglionic
- benzilate
-
somata
-
calretinin
-
wga-hrp
-
intermediolateral
- broca
- analysis
-
amacrine
-
ache-positive
- pharmacology
-
pedunculopontine
-
ibotenic
- diagnostics
- tegmentum
- medicine
The taxonomic range for the selected organisms is: Drosophila melanogaster
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
choline acetyltransferase, choline acetyl transferase, pchat, choline-acetyltransferase, cchat, choline acetylase, choline o-acetyltransferase, acetyl-coa:choline o-acetyltransferase, peripheral type of choline acetyltransferase, acetyl-coa:choline-o-acetyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyl CoA:choline-O-acetyltransferase
-
-
-
-
acetyl-CoA:choline-O-acetyltransferase
-
-
-
-
acetyltransferase, choline
-
-
-
-
chAcT
-
-
-
-
choline acetyl transferase
-
-
-
-
choline acetylase
-
-
-
-
choline acetyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:choline O-acetyltransferase
Propanoyl-CoA can act, more slowly, in place of acetyl-CoA.
CAS REGISTRY NUMBER
COMMENTARY
9012-78-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + choline
acetylcholine + CoA
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
direct interaction between the kinesin-2 motor and ChAT for brief duration induces the episodic flow towards synapse, and synaptic activity is essential for this interaction. Blocking the acetylcholine synthesis through the HC3 treatment, and activation of the post synaptic neurons through the inhibition of actylcholine receptors by BTX, respectively, reduce the axonal entry and disrupt the episodic nature of ChAT transport within a short time
physiological function
SRSF/SR protein B52 function is required for ChATsplicing. At the end of embryogenesis, loss of B52 function impedes splicing of ChAT, reduces acetylcholine synthesis, and extends the period of uncoordinated muscle twitches during larval hatching
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CLAT_DROME
721
0
81328
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
13000
-
1 * 54000 + 1 * 13000, major form isolated, may be generated from monomeric form by limited proteolysis, SDS-PAGE
54000
67000
67000 - 69000
-
gel filtration, sucrose density gradient centrifugation
68000
-
1 * 68000, enzyme is initially synthesized as 75 kDa precursor-protein, SDS-PAGE
54000
-
1 * 54000 + 1 * 13000, major form isolated, may be generated from monomeric form by limited proteolysis, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
1 * 54000 + 1 * 13000, major form isolated, may be generated from monomeric form by limited proteolysis, SDS-PAGE
monomer
monomer
-
1 * 68000, enzyme is initially synthesized as 75 kDa precursor-protein, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chao, L.P.
Choline acetyltransferase: purification and characterization
J. Neurosci. Res.
5
85-115
1980
Bos taurus, Drosophila melanogaster, Homo sapiens, Rattus norvegicus, Tetronarce californica
Slemmon, J.R.; Salvaterra, P.M.; Crawford, G.D.; Roberts, E.
Purification of choline acetyltransferase from Drosophila melanogaster
J. Biol. Chem.
257
3847-3852
1982
Drosophila melanogaster
Slemmon, J.R.; Salvaterra, P.M.; Roberts, E.
Molecular characterization of choline acetyltransferase from Drosophila melanogaster
Neurochem. Int.
6
519-525
1984
Drosophila melanogaster
Carbini, L.A.; Hersh, L.B.
Functional analysis of conserved histidines in choline acetyltransferase by site-directed mutagenesis
J. Neurochem.
61
247-253
1993
Caenorhabditis elegans, Drosophila melanogaster, Rattus norvegicus, Sus scrofa
Liu, B.; Bossing, T.
Single neuron transcriptomics identify SRSF/SR protein B52 as a regulator of axon growth and choline acetyltransferase splicing
Sci. Rep.
6
34952
2016
Drosophila melanogaster (P07668)
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