Information on EC 2.3.1.6 - choline O-acetyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
2.3.1.6
-
RECOMMENDED NAME
GeneOntology No.
choline O-acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
acetyl-CoA + choline = CoA + O-acetylcholine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Glycerophospholipid metabolism
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:choline O-acetyltransferase
Propanoyl-CoA can act, more slowly, in place of acetyl-CoA.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
acetyl CoA:choline-O-acetyltransferase
-
-
-
-
acetyl-CoA:choline-O-acetyltransferase
-
-
-
-
acetyltransferase, choline
-
-
-
-
cChAT
-
common choline O-acetyltransferase
cChAT
-
common choline O-acetyltransferase
cChAT
-
common type choline acetyltransferase
chAcT
-
-
-
-
ChAT
-
-
ChAT
Oenanthe siolonifera, Oryza sativa, Paeonia suffruticosa
-
-
ChAT
Paeonia suffruticosa Andrews
-
-
-
ChAT
Polygonatum sibiricum Red.
-
-
-
ChAT
-
-
ChAT
Poria cocos Wolf.
-
-
-
ChAT
Rosa laevigata Michx
-
-
-
ChAT
-
-
choline acetyl transferase
-
-
-
-
choline acetylase
-
-
-
-
choline acetyltransferase
-
-
-
-
choline acetyltransferase
-
-
choline acetyltransferase
-
-
choline acetyltransferase
-
-
choline acetyltransferase
-
-
choline acetyltransferase
-
-
choline acetyltransferase
-
-
choline acetyltransferase
-
-
choline acetyltransferase
-
-
choline acetyltransferase
-
-
choline acetyltransferase
-
-
choline acetyltransferase
-
-
choline acetyltransferase
Oenanthe siolonifera, Oryza sativa, Paeonia suffruticosa
-
-
choline acetyltransferase
Paeonia suffruticosa Andrews
-
-
-
choline acetyltransferase
-
-
choline acetyltransferase
-
-
choline acetyltransferase
Polygonatum sibiricum Red.
-
-
-
choline acetyltransferase
-
-
choline acetyltransferase
Poria cocos Wolf.
-
-
-
choline acetyltransferase
-
-
choline acetyltransferase
-
-
choline acetyltransferase
-
-
choline acetyltransferase
Rosa laevigata Michx
-
-
-
choline acetyltransferase
-
-
choline acetyltransferase
-
-
pChAT
-
peripheral choline O-acetyltransferase, predominantly found in peripheral neurons
pChAT
-
a variant form of choline acetyltransferase
pChAT
-
peripheral choline O-acetyltransferase, predominantly found in peripheral neurons
pChAT
-
splice variant of choline acetyltransferase
CAS REGISTRY NUMBER
COMMENTARY
9012-78-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
2 enzyme forms
-
-
Manually annotated by BRENDA team
colocalization of calbindin-D28k and calretinin with ChAT
-
-
Manually annotated by BRENDA team
goldfish
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
var. ma-yuen
-
-
Manually annotated by BRENDA team
zebrafish mutant line, bajan, in which compromised motility and fatigue result from a point mutation in the gene coding choline acetyltransferase
Uniprot
Manually annotated by BRENDA team
snail
-
-
Manually annotated by BRENDA team
horseshoe crab
-
-
Manually annotated by BRENDA team
Lepidoptera: Spingidae
-
-
Manually annotated by BRENDA team
3 enzyme forms
-
-
Manually annotated by BRENDA team
B6 CBA wild type mice
-
-
Manually annotated by BRENDA team
Musa domestica
-
-
-
Manually annotated by BRENDA team
Oenanthe siolonifera
-
-
-
Manually annotated by BRENDA team
Paeonia suffruticosa Andrews
Andrews
-
-
Manually annotated by BRENDA team
3 enzyme forms
-
-
Manually annotated by BRENDA team
Polygonatum sibiricum Red.
Red.
-
-
Manually annotated by BRENDA team
Wolf.
-
-
Manually annotated by BRENDA team
Poria cocos Wolf.
Wolf.
-
-
Manually annotated by BRENDA team
var. ansu
-
-
Manually annotated by BRENDA team
Sprague Dawley rats
-
-
Manually annotated by BRENDA team
two splicing variants, peripheral-type pChAT and common-type cChAT
-
-
Manually annotated by BRENDA team
Rosa laevigata Michx
Michx
-
-
Manually annotated by BRENDA team
Sasamorpha purpurascens
-
-
-
Manually annotated by BRENDA team
ChAT/calretinin colocalization
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
mutations in the superoxide dismutase 1, sod1, gene cause familial amyotrophic lateral sclerosis and motor axons in SOD1G93A-Tg mice also show a reduction in ChAT transport from the pre-onset stage, microtubule-dependent release of acetylcholine is significantly impaired by misfolded SOD1 species, overview. Sequestration by misfolded SOD1 species results in inhibition of ChAT transport, which plays a role in amyotrophic lateral sclerosis, overview
malfunction
-
in cigarette smokers and patients with chronic obstructive pulmonary disease, acetylcholine activation in lung fibroblasts causes increased cell proliferation involving muscarinic M1, M2, and M3 receptors, and ERK1/2 and NFkappaB pathways, overview
physiological function
-
ChAT is the rate-limiting enzyme of generating acetylcholine, which is synthesized in cholinergic neuronal cell bodies. Insulin signaling may play an important part in the activities of cholinergic neurons
physiological function
-
acetylcholine, synthesized by ChAT, and muscarinic M1, M2, and M3 receptors are involved in fibroblast proliferation
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + carnitine
acetylcarnitine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + carnitine
acetylcarnitine + CoA
show the reaction diagram
-
a mutant enzyme that incorporates four amino acid substitutions from wild type, shows a substantial increase in catalytic efficiency toward L-carnitine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
P32738
-
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
Musa domestica
-
-
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
kinetic data indicate that choline acetyltransferase operates by forming an acetylated enzyme as an intermediate in the reversible reaction between acetyl-CoA and choline
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
synthesis of the neurotransmitter acetylcholine that is essential for the development and neuronal activities of the cholinergic systems involved in many fundamental brain functions
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
synthesis of the neurotransmitter acetylcholine, deficiency in ChAT involved in several neurological and psychiatric disorders
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
P32738
synthesis of the neurotransmitter acetylcholine, mutations in ChAT causes congenital neuromuscular disorders
-
-
r
acetyl-CoA + choline
CoA + O-acetylcholine
show the reaction diagram
-
-
-
-
?
acetyl-CoA + choline
CoA + O-acetylcholine
show the reaction diagram
-
-
-
-
?
acetyl-CoA + choline
CoA + O-acetylcholine
show the reaction diagram
-
-
-
-
?
acetyl-CoA + choline
CoA + O-acetylcholine
show the reaction diagram
-
-
acetylcholine is the primary parasympathetic neurotransmitter in the airways
-
?
acetyl-CoA + choline
CoA + O-acetylcholine
show the reaction diagram
-
choline taken up by OCTs or derived from the plasma membrane is also utilized for acetylcholine synthesis in both cholinergic neurons and nonneuronal cholinergic cells, such as lymphocytes
-
-
?
acetyl-CoA + choline
CoA + O-acetylcholine
show the reaction diagram
-
formation of acetylcholine in cholinergic neurons largely depends on both the levels of choline being transported into the cells from the extracellular space and the activity of ChAT, kinetics of choline uptake in the SK-N-SH cells
acetylcholine is the neurotransmitter used by cholinergic neurons
-
?
additional information
?
-
-
pilocarpine-induced seizures produce alterations on choline acetyltransferase and acetylcholinesterase activities and deficit memory in rats, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
-
-
-
-
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
synthesis of the neurotransmitter acetylcholine that is essential for the development and neuronal activities of the cholinergic systems involved in many fundamental brain functions
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
synthesis of the neurotransmitter acetylcholine, deficiency in ChAT involved in several neurological and psychiatric disorders
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
P32738
synthesis of the neurotransmitter acetylcholine, mutations in ChAT causes congenital neuromuscular disorders
-
-
r
acetyl-CoA + choline
CoA + O-acetylcholine
show the reaction diagram
-
-
-
-
?
acetyl-CoA + choline
CoA + O-acetylcholine
show the reaction diagram
-
-
-
-
?
acetyl-CoA + choline
CoA + O-acetylcholine
show the reaction diagram
-
-
acetylcholine is the primary parasympathetic neurotransmitter in the airways
-
?
acetyl-CoA + choline
CoA + O-acetylcholine
show the reaction diagram
-
choline taken up by OCTs or derived from the plasma membrane is also utilized for acetylcholine synthesis in both cholinergic neurons and nonneuronal cholinergic cells, such as lymphocytes
-
-
?
acetyl-CoA + choline
CoA + O-acetylcholine
show the reaction diagram
-
formation of acetylcholine in cholinergic neurons largely depends on both the levels of choline being transported into the cells from the extracellular space and the activity of ChAT, kinetics of choline uptake in the SK-N-SH cells
acetylcholine is the neurotransmitter used by cholinergic neurons
-
?
additional information
?
-
-
pilocarpine-induced seizures produce alterations on choline acetyltransferase and acetylcholinesterase activities and deficit memory in rats, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K+
-
highest activity at 10-20 mM K+
additional information
-
addition of K+ does not affect activity
additional information
-
metal binding site found in crystal structure analysis, bound metal is most likely a Na+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-Bromoacetonyltrimethylammonium bromide
-
-
3-Bromoacetonyltrimethylammonium ion
-
-
3-Trimethylammoniomethylcatechol
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
Acetylaminocholine
-
-
Acetylcholine
-
-
Acetylcholine
-
competitive to choline, non-competitive to acetyl-CoA
amyloid beta peptide
-
the aggregated form of A-beta 25-35 decreased significantly enzyme activity only in the aged striatum
-
arachidonic acid
-
-
bromo-acetylcholine
-
-
Bromoacetyl-S-CoA
-
-
bromoacetylcholine
-
a selective inhibitor of choline acetyltransferase
Catecholine
-
-
Chlorocholine
-
-
Choline mustard aziridinium salt
-
-
CoA
-
competitive to acetyl-CoA, non-competitive to choline
dexamethasone
-
-
Diethylaminoethanol
-
-
diethyldicarbonate
-
-
domoic acid
-
-
ethylenimine
-
-
Flubenzimine
-
i.e. N-[3-phenyl-4,5-bis[(trifluoromethyl)immino]-2-thiazolidinylidene]benzenamine
glutamate
-
-
Hg2+
-
noncompetitive with respect to choline, IC50: 0.0004 mM, mixed type inhibition with respect to acetyl-CoA, IC50: 0.0025 mM, activity can be recovered using 2,3-dimercapto-propanol
iodoacetamide
-
-
iodoacetate
-
-
N,N-Dimethylaminoethyl acrylate
-
-
N,N-Dimethylaminoethyl bromoacetate
-
-
N,N-Dimethylaminoethyl chloroacetate
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
the enzyme is completely protected against N-ethylmaleimide inactivation by acetyl coenzyme A and is substantially protected by acetyl choline
N-Hexamethylene-4-(1-naphthylvinyl)pyridinium-6-trimethylammonium ion
Bos taurus, Musa domestica
-
-
-
N-Methyl-4-(1-naphthylvinyl)pyridine
-
-
N-Methyl-4-(1-naphthylvinyl)pyridine
-
-
N-Methyl-4-(1-naphthylvinyl)pyridine
Musa domestica
-
-
N-Methyl-4-(1-naphthylvinyl)pyridine
-
-
nerve growth factor
-
nerve growth factor, under specific development conditions, leads to a paradoxical down-regulation of the enzyme
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
phenylacetate
-
-
phenylacetyl-CoA
-
-
phenylbutyrate
-
-
Phenylmethanesulfonylfluoride
-
-
pilocarpine
-
pilocarpine-induced seizures reduce choline acetyltransferase activity in the hippocampus, overview
pilocarpine
-
decreases the enzyme activity in the hippocampus, lipoic acid protects, overview
pilocarpine
-
the enzyme activity in striatum and frontal cortex is reduced after pilocarpine-induced seizures
quisqualate
-
-
Styrylpyridinium salts
-
-
Styrylpyridinium salts
Musa domestica
-
-
thioctic acid
-
it is proposed that dihydrolipoic acid serves an essential role in the regulation of the activity of the the enzyme and that the ratio of reduced to oxidized lipoic acid in the cell may play an important role in the regulation of the activity of the enzyme
veratridine
-
-
Zinc acetate
-
-
[2-[3-(2-Ammonioethoxy)-benzoyl]ethyl]trimethylammonium bromide
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
C3d
-
a neural cell adhesion molecule ligand, 65-74% activation at 0.001 mM involving the fibroblast growth factor receptor, activation is inhibited by the FGFR inhibitor, SU5402
-
choline
-
extracellular choline increases acetylcholine contents in the cell
Cl-
-
enzyme activity increases in the presence of ionic strength, Cl- is the most potent activator in comparison with Br-and I-
Creatinine-HCl
-
-
Dihydrolipoic acid
-
it is proposed that dihydrolipoic acid serves an essential role in the regulation of the activity of the the enzyme and that the ratio of reduced to oxidized lipoic acid in the cell may play an important role in the regulation of the activity of the enzyme
Guanidine-HCl
-
-
high-affinity choline transporter
-
i.e. CHT1, plays a key role in acetylcholine synthesis and choline uptake, CHT1 inhibition also inhibits acetylcholine formation, overview
-
kinesin-associated protein 3
-
i.e. KAP3, is a kinesin-2 subunit responsible for binding to cargos including choline acetyltransferase. Sequestration by misfolded SOD1 species results in inhibition of ChAT transport
-
lipoic acid
-
lipoic acid and pilocarpine together increase enzyme activity in the hippocampus of healthy and epileptic rats, lipoic acid alone does not alter hippocampal ChAT activity. Lipoic acid protects rats against pilocarpine-induced seizures and eliminates lethality, overview
NGFI-A
-
NGF activates transcriptional factors which influence the promotor region of the enzyme
-
NGFI-C
-
NGF activates transcriptional factors which influence the promotor region of the enzyme
-
okadaic acid
-
increases the activity of water-soluble and nonionically membrane-bound enzyme
pilocarpine
-
lipoic acid and pilocarpine together increase enzyme activity in the hippocampus of healthy and epileptic rats, lipoic acid alone does not alter hippocampal ChAT activity. Lipoic acid protects rats against pilocarpine-induced seizures and eliminates lethality, overview
sarin
-
choline acetyltransferase activity is increased in cortex, brainstem and midbrain 6h after LD50 treatment, and the elevated enzyme activity persisted up to 20h after treatment
Sodium acetate
-
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00201
-
acetyl-CoA
-
cosubstrate carnitine
0.00284
-
acetyl-CoA
-
enzyme mutant ChAT-R/TET, cosubstrate carnitine
0.0082
0.032
acetyl-CoA
-
-
0.012
-
acetyl-CoA
-
enzyme mutant ChAT-R, cosubstrate carnitine
0.0148
-
acetyl-CoA
-
enzyme mutant ChAT-TET, cosubstrate carnitine
0.015
-
acetyl-CoA
-
cosubstrate choline
0.0155
-
acetyl-CoA
-
enzyme mutant ChAT-R, cosubstrate choline
0.016
-
acetyl-CoA
-
-
0.0225
-
acetyl-CoA
-
enzyme mutant ChAT-TET, cosubstrate choline
0.029
-
acetyl-CoA
-
-
0.051
-
acetyl-CoA
-
-
0.0516
-
acetyl-CoA
-
enzyme mutant ChAT-R/TET, cosubstrate acetyl-CoA
0.055
-
acetyl-CoA
-
-
0.068
-
acetyl-CoA
-
-
0.12
-
acetyl-CoA
-
-
0.221
-
acetyl-CoA
-
-
5
-
acetyl-CoA
-
-
0.0004
-
Acetylcholine
-
-
0.0011
-
Acetylcholine
-
enzyme mutant R463A
0.0015
-
Acetylcholine
-
enzyme mutant R453A
0.002
-
Acetylcholine
-
enzyme mutant R458A
0.0092
-
Acetylcholine
-
enzyme mutant R452A
0.67
-
Acetylcholine
-
enzyme mutant H393N
1.7
-
Acetylcholine
-
enzyme mutant H268L
2
-
Acetylcholine
-
-
2.1
-
Acetylcholine
-
-
2.7
-
Acetylcholine
-
enzyme mutant H268N
4.8
-
carnitine
-
enzyme mutant ChAT-R/TET, cosubstrate acetyl-CoA
100
-
carnitine
-
cosubstrate acetyl-CoA; enzyme mutant ChAT-R, cosubstrate acetyl-CoA; enzyme mutant ChAT-TET, cosubstrate acetyl-CoA
0.192
-
choline
-
cosubstrate acetyl-CoA
0.299
-
choline
-
-
0.33
-
choline
-
-
0.37
-
choline
-
-
0.66
-
choline
-
-
0.88
-
choline
-
-
1.88
-
choline
-
enzyme mutant ChAT-R, cosubstrate acetyl-CoA
2
-
choline
-
-
3.5
-
choline
-
-
4.4
19
choline
-
-
4.4
-
choline
-
-
5.79
-
choline
-
enzyme mutant ChAT-TET, cosubstrate acetyl-CoA
128
-
choline
-
enzyme mutant ChAT-TET, cosubstrate acetyl-CoA
0.00025
-
CoA
-
-
0.0004
-
CoA
-
enzyme mutant R458A
0.001
-
CoA
-
enzyme mutant R453A
0.0016
-
CoA
-
enzyme mutant R463A
0.014
-
CoA
-
enzyme mutant H268N
0.0154
-
CoA
-
enzyme mutant R452A
0.017
-
CoA
-
enzyme mutant H393N
0.025
-
CoA
-
-
0.04
-
CoA
-
enzyme mutant H268L
additional information
-
additional information
-
overview
-
additional information
-
additional information
-
overview
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
dependence on salt concentration
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
temperature dependence
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
15
-
3-trimethylammoniomethyl catechol
-
-
25
-
Catecholine
-
-
0.008
-
coenzyme A
-
-
0.0005
-
Hg2+
-
pH 7.4, 37°C
0.00031
-
phenylacetyl-CoA
-
-
0.8
-
thioctic acid
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0025
-
Hg2+
-
noncompetitive with respect to choline, IC50: 0.0004 mM, mixed type inhibition with respect to acetyl-CoA, IC50: 0.0025 mM, activity can be recovered using 2,3-dimercapto-propanol
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50
-
-
purified enzyme, pH 7.4
142
-
-
-
additional information
-
-
overview: assay methods
additional information
-
-
overview: assay methods
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.3
-
-
without NaCl in assay medium
7
8
-
presence of NaCl
7.2
-
-
-
7.4
-
-
-
7.4
-
-
assay at
8.3
-
-
-
additional information
-
-
broad optimum in alkaline range
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
37
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
developing antenna during larvae development, enzyme detected in neurons, glia and epidermal cells
Manually annotated by BRENDA team
Musa domestica
-
-
Manually annotated by BRENDA team
-
caudate nuleus
Manually annotated by BRENDA team
-
regional distribution
Manually annotated by BRENDA team
-
brainstem, midbrain; cortex
Manually annotated by BRENDA team
-
cerebral cortex
Manually annotated by BRENDA team
-
cortex; triatum
Manually annotated by BRENDA team
-
ingestion of lower quantity and quality of dietary protein are likely to control the mRNA level and concentration of NGF, and cause a decline in the activity of choline acetyltransferase in the brains of young rats
Manually annotated by BRENDA team
-
colocalization of nitric oxide synthase and choline acetyltransferase. nNOS/ChAT-positive cells are detected in: the diencephalon (the preoptic and suprachiasmatic nuclei, the habenula, the dorsal thalamus, and the nucleus of the medial longitudinal fasciculus), the mesencephalon (the optic tectum, the mesencephalic portion of the trigeminal nucleus, the oculomotor and trochlear nuclei, and the Edinger-Westphal nucleus) and the rhombencephalon (the secondary gustatory nucleus, the nucleus isthmi, the lateral lemniscus nucleus, the cerebellum, the reticular formation, different nuclei of the octaval column, the motor zone of the vagal lobe, and the trigeminal, facial, abducens, glosso-pharyngeal, vagal, and hypobranchial motor nuclei). Double-labeled cells are also observed in the spinal motor column
Manually annotated by BRENDA team
-
silencing of choline acetyltransferase expression by lentivirus-mediated RNA interference
Manually annotated by BRENDA team
-
cChAT and pChAt expression analysis in brain, overview
Manually annotated by BRENDA team
-
pChAT+ nerve fibers are found exclusively in the trigeminal and solitary systems. The ventral portion of the principal sensory nucleus contains many pChAT+ fibers
Manually annotated by BRENDA team
-
33% of activity membrane associated
Manually annotated by BRENDA team
-
ChAT activity is higher in Ts65Dn mice at both 19 and 24 months of age compared to normogenic animals
Manually annotated by BRENDA team
-
lung, fetal lung fibroblasts, HFL-1
Manually annotated by BRENDA team
-
impaired spatial working memory and altered choline acetyltransferase immunoreactivity and nicotinic receptor binding in rats exposed to intermittent hypoxia during sleep
Manually annotated by BRENDA team
-
64% of activity membrane associated
Manually annotated by BRENDA team
-
exposure to enriched environment improves spatial learning performances and enhances cell density but not choline acetyltransferase activity in the hippocampus of ventral subicular-lesioned rats
Manually annotated by BRENDA team
-
in both young adult and middle-aged animals, oestradiol treatment initiates immediately after ovariectomy significantly increased ChAT levels in the hippocampus but not in the prefrontal cortex compared to cholesterol control treatment. When oestradiol treatment is initiated 5 months after ovariectomy, it fails to significantly increase ChAT levels in the hippocampus, but does so in the prefrontal cortex
Manually annotated by BRENDA team
-
increased ChAT activity in some brain regions, notably the hippocampus, of patients diagnosed with mild cognitive impairment
Manually annotated by BRENDA team
-
ChAT activity is increased at 10 and 12 months of age in the hippocampus of Ts65Dn mice compared to normogenic animals
Manually annotated by BRENDA team
-
cholinergic neuron-specific ChAT in the CA1 region of hippocampus
Manually annotated by BRENDA team
-
ChAt activity in untreated and in pilocarpine-treated hippocampi, overview
Manually annotated by BRENDA team
-
15% of activity membrane associated
Manually annotated by BRENDA team
-
strong pChAT signal in intrinsic primary afferent neurons, low immunoreactivity for cChAT
Manually annotated by BRENDA team
-
transgenic
Manually annotated by BRENDA team
-
cholinergic neurons
Manually annotated by BRENDA team
-
cholinergic neurons; Dogiel type II cell, strongest pChAT signal
Manually annotated by BRENDA team
-
pChAT predominantly in peripheral neurons
Manually annotated by BRENDA team
-
trigeminal neuron, the majority of pChAT-positive neurons has small to medium-sized cell bodies. More than 90% of substance P (SP)-positive trigeminal cells and about 80% of calcitonin gene-related peptide (CGRP)-positive cells exhibited pChAT-immunoreactivity. pChAT-positive cells form a larger population of neurons than SP-positive or CGRP-positive cells, but they are a different population from calbindin-D28k-positive neurons. pChAT-immunoreactivity is present in a subset of neurons positive for neuronal nitric oxide synthase. pChAT plays roles not only in nociception, but also in other sensory functions such as mechanoreception mediating tactile sensation
Manually annotated by BRENDA team
-
Alzheimer’s disease/galanin+ cells display a significant upregulation in choline acetyltransferase mRNA expression compared to cognitive impairment and Alzheimer’s disease/galanin- cells. Galanin fiber hyperinnervation of cholinergic nucleus basalis neurons upregulates the expression of ChAT
Manually annotated by BRENDA team
-
ChAT+/NOS- neurons account for 48% of myenteric neurons and ChAT-/NOS+ neurons accounted for 43%. ChAT+/NOS+ neurons comprised 4% of the total number of neurons. ChAT-/NOS- neurons comprise 5% of all cells
Manually annotated by BRENDA team
-
in addition, to the somatomotor neurons and the intermediolateral column, throughout the spinal cord small ChATir cells are found in the central ventral gray but not in the dorsal gray
Manually annotated by BRENDA team
-
cholinergic
Manually annotated by BRENDA team
-
; cholinergic
Manually annotated by BRENDA team
-
septal cholinergic
Manually annotated by BRENDA team
-
silencing of choline acetyltransferase expression by lentivirus-mediated RNA interference
Manually annotated by BRENDA team
-
non-neuronal cholinergic cell
Manually annotated by BRENDA team
-
no significant differences of ChAT activity are measured at both 19 and 24 months of age between Ts65Dn mice and normogenic animals
Manually annotated by BRENDA team
-
no significant differences of ChAT activity are measured at both 19 and 24 months of age between Ts65Dn mice and normogenic animals
Manually annotated by BRENDA team
-
enzyme-containing neuronal cell bodies in only two regions, the cell islands of the optic lobe medulla and the cortical layer of the posterior olfactory lobule. Immunoreactive fibers and probable nerve terminals are found in the plexiform layer of the deep retina, within the stroma of the optic gland, and the neuropils of the optic lobe, peduncle lobe, and olfactory lobe
Manually annotated by BRENDA team
-
enzyme-containing neuronal cell bodies in only two regions, the cell islands of the optic lobe medulla and the cortical layer of the posterior olfactory lobule. Immunoreactive fibers and probable nerve terminals are found in the plexiform layer of the deep retina, within the stroma of the optic gland, and the neuropils of the optic lobe, peduncle lobe, and olfactory lobe
Manually annotated by BRENDA team
-
enzyme-containing neuronal cell bodies in only two regions, the cell islands of the optic lobe medulla and the cortical layer of the posterior olfactory lobule. Immunoreactive fibers and probable nerve terminals are found in the plexiform layer of the deep retina, within the stroma of the optic gland, and the neuropils of the optic lobe, peduncle lobe, and olfactory lobe
Manually annotated by BRENDA team
-
in both young adult and middle-aged animals, oestradiol treatment initiates immediately after ovariectomy significantly increased ChAT levels in the hippocampus but not in the prefrontal cortex compared to cholesterol control treatment. When oestradiol treatment is initiated 5 months after ovariectomy, it fails to significantly increase ChAT levels in the hippocampus, but does so in the prefrontal cortex
Manually annotated by BRENDA team
-
ChAT protein levels are significantly increased in the dark-reared retina compared to those of the control. Light deprivation increases the expression of ChAT, increasing the apparent density of cholinergic neurons in the developing turtle retina
Manually annotated by BRENDA team
-
enzyme-containing neuronal cell bodies in only two regions, the cell islands of the optic lobe medulla and the cortical layer of the posterior olfactory lobule. Immunoreactive fibers and probable nerve terminals are found in the plexiform layer of the deep retina, within the stroma of the optic gland, and the neuropils of the optic lobe, peduncle lobe, and olfactory lobe
Manually annotated by BRENDA team
-
only a few ChATir neurons are found outside the somatomotor groups in the ventral gray
Manually annotated by BRENDA team
-
in addition, to the somatomotor neurons and the intermediolateral column, throughout the spinal cord small ChATir cells are found in the central ventral gray but not in the dorsal gray
Manually annotated by BRENDA team
-
motor neurons
Manually annotated by BRENDA team
-
the ganglion neurons possess pChAT, but never cChAT, mRNA and protein. pChAT has enzyme activity enough to supply physiological concentrations of acetylcholine in the ganglion. pChAT contributes both to acetylcholine neurotransmission in physiologically identified cholinergic cells and to functions yet unknown in non-cholinergic neurons
Manually annotated by BRENDA team
-
pChAT occurs in most CGRP+ SP+ ganglion cells, such sparseness of pChAT+ fibers implies poor transportation of pChAT to axon branchlets
Manually annotated by BRENDA team
-
dorsal motor nucleus of the vagus nerve, contains a peripheral-type pChAT, a splice variant that lacks exons 6-9 of the common-type ChAT, cChAT
Manually annotated by BRENDA team
additional information
-
immunofluorescent localization study, overview
Manually annotated by BRENDA team
additional information
-
after axotomy pChAT immunoreactivity is apparent in some brainstem nuclei, such as the dorsal motor nucleus of the vagus nerve, the nucleus ambiguus, and the hypoglossal nucleus, but not in the brainstem neurons of normal rats
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
cChAT but not pChAT, pChAT found in nucleus only after treatment with leptomycin B
Manually annotated by BRENDA team
-
associated with synaptic vesicles, can be displaced by treatment with urea or alkaline solutions
Manually annotated by BRENDA team
-
80-90% of total activity
-
Manually annotated by BRENDA team
-
primary form
-
Manually annotated by BRENDA team
-
ChAT transport in the microtubule, schematic overview
Manually annotated by BRENDA team
additional information
-
immunofluorescent localization study, overview
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30000
300000
-
self-association to large aggregates, gel filtration, sedimentation equilibrium
49000
-
-
pChAT
66800
-
-
gel filtration
67000
69000
-
gel filtration, sucrose density gradient centrifugation
67000
69000
-
native PAGE
67000
69000
-
gel filtration
67000
69000
-
gel filtration
68000
-
-
gel filtration
69000
-
-
cChAT
71000
-
-
gel filtration
76000
-
-
pChAT with GFP as fusion protein
80000
-
-
gel filtration
96000
-
-
cChAT with GFP as fusion protein
106000
-
-
largest aggregate, formation after ammonium sulfate fractionation, gel filtration
120000
125000
-
peaks A, B1, gel filtration, gel electrophoresis
128000
-
-
gel filtration
140000
-
-
gradient polyacrylamide electrophoresis
200000
-
-
peak B2, gel filtration, gel electrophoresis
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 68300, SDS-PAGE
?
-
x * 72000, isozyme CAT-A, x * 76000, isozyme CAT-B, SDS-PAGE
?
-
x * 54000 + x * 67000, SDS-PAGE
?
-
x * 62000, form 1, x * 67000, form 2, SDS-PAGE
?
-
dimer or tetramer: 2 * 68000 or 4 * 34000, SDS-PAGE
?
-
x * 37000 + x * 56000, SDS-PAGE, ultracentrifugation in presence of guanidine-HCl
?
-
x * 69000 + x * 34000, SDS-PAGE
dimer
-
1 * 54000 + 1 * 13000, major form isolated, may be generated from monomeric form by limited proteolysis, SDS-PAGE
dimer
-
chicken enzyme consists of 2 subunits of identical molecular weight
dimer
-
2 * 42000, SDS-PAGE
monomer
-
1 * 68500, SDS-PAGE
monomer
-
1 * 65000, SDS-PAGE
monomer
-
1 * 67000, SDS-PAGE
monomer
-
1 * 66000, SDS-PAGE
monomer
-
1 * 66000, SDS-PAGE
monomer
-
1 * 68000, enzyme is initially synthesized as 75 kDa precursor-protein, SDS-PAGE
monomer
-
crystal structure analysis
monomer
-
gel filtration, dimerization caused by oxidation can be reversed by addition of reducing agents
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
serine 440 of the recombinant human 69-kDa protein is the phoshorylation site
phosphoprotein
-
rat choline acetyltransferase is phosphorylated in Sf9 cells
phosphoprotein
-
-
phosphoprotein
-
phosphorylation enables membrane association
phosphoprotein
-
regulation of activity by phosphorylation
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapor diffusion method
-
sitting drop vapor diffusion method
-
vapor diffusion crystallization
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
60% sucrose, 1 mg/ml bovine serum albumin, 2 h stable
additional information
-
-
increasing ionic strength increases susceptibility to thermal degradation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
bovine serum albumin stabilizes
-
bovine serum albumin stabilizes
-
EDTA stabilizes
-
sucrose stabilizes
-
bovine serum albumin stabilizes
-
EDTA stabilizes
-
sucrose stabilizes
-
acetyl-CoA stabilizes
-
choline chloride stabilizes
-
increasing ionic strength increases susceptibility to proteolysis and thermal degradation
-
bovine serum albumin stabilizes
-
ethylene glycol stabilizes
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
extremely sensitive to oxidation due to its cysteine-rich nature, oxidation causes formation of dimers and loss of activity
-
660442
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20°C, partially purified preparation, several months stable, less stable in purified state
-
-20°C, several months
-
4°C, 24 h, less than 10% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2 isozymes
-
overview procedures
-
overview procedures
-
placental acidic and basic form
-
recombinant proteins using His-tag or chitin-binding-domain
-
recombinant enzyme using His-tag
-
large scale
-
overview procedures
-
overview procedures
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
expression of wild-type- and S440A mutant-enzyme in HEK293 cells
-
large-scale expression as His-tag or chitin-binding-domain fusion protein in Escherichia coli, His-tag fusion protein expresses in inclusion bodies at 37°C growth temperature and in soluble form at 20°C, chitin-binding-domain fusion protein expressed at 15°C but not at 37°C
-
two fragments of the hChAT gene are used for functional analysis carrying 944 bp (P1) and 4000 bp (P2) of the 5' flanking region in front of the chloramphenicol acetyltransferase (CAT) reporter gene. They are transfected in NG108-15, SN6 and COS-1 cells
-
stable expression of the enzyme in NIH-3T3 fibroblasts, expression of ChAT and high-affinity choline transporter CHT1 in NIH-3T3 cells giving NIH3T3ChAT 112-1 cells leading to increased binding of the CHT1 inhibitor hemicholinium-3 and greater choline uptake and acetylcholine synthesis compared to NIH3T3ChAT 103-1 cells, a CHT1-negative control cell line
-
cDNAs encoding splicing variants cChAT and pChAT, purified from the rat striatum and pterygopalatine ganglion, respectively, expression analysis. Recombinant expression in HEK-293 cells
-
expressed as GFP fusion protein in HEK293 cells
-
expressed in Escherichia coli B834
-
expression in FR3T3 fibroblasts, SN6 cells and transgenic mice, a 3800-bp 5'flanking segment from the rat ChAT gene promotor directed cell type-specific expression of a reporter gene in cholinergic cells. A 2342-bp segment from the 5' flanking region of the ChAT gene behaves as an enhancer in cholinergic cells but as a repressor in noncholinergic cells in an orientation-independent manner
-
expression in Spodoptera frugiperda Sf9 cells; expression in Spodoptera frugiperda Sf9 cells using a baculovirus expression system
-
residues 18-617 of full length DNA expressed in Escherichia coli DH5alphaF’IQ
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
interleukin-1beta induces the enzyme in HFL-1 cells
-
scopolamine suppresses the enzyme in neurons
-
pChAT expression is induced by neuronal damage
-
Nelumbo nucifera semen extract improves memory in rats with scopolamine-induced amnesia through the induction of choline acetyltransferase expression
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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
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
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
real-time multiplex PCR technique can be carried out in a single tube and can differentiate between the polymorphic sites of the ChAT gene associated with Alzheimer’s disease
medicine
P28329
investigation of three ChAt gene polymorphisms in schizophrenia. Evidence for an influence of a 5' promoter polymorphism, rs1880676A/G, on susceptibility to the disorder among individuals of Basque origin. Evidence for a similar though less significant, influence for a second polymorphism of putative function, rs3810950
medicine
-
ChAT 2384 A allele is a risk factor for Alzheimer’s disease and mild cognitive impairment
medicine
-
a severe case of congenital myasthenia gravis in a Chinese newborn is reported who presents with complete ptosis, severe hypotonia, dysphagia and respiratory insufficiency with recurrent apnea that requires mechanical ventilatory support since birth. The infant has heterozygous mutations in the choline acetyltransferase genes, p.T553N and p.S704P
diagnostics
-
ChAT is selected as a marker of cholinergicneurons. In the CA1 region of hippocampus of mice, several of the insulin signaling-related proteins are co-located with ChAT, and most double immunoreactive positive cells are pyramidal cells
medicine
-
promoting ChAT activity and acetylcholine release can lead to treatments for neurodegenerative diseases with cholinergic deficits, such as Alzheimer’s disease
pharmacology
-
Nelumbo nucifera semen extract improves memory in rats with scopolamine-induced dementia through the induction of choline acetyltransferase expression and inhibition of acetylcholinesterase activity