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Information on EC 2.3.1.6 - choline O-acetyltransferase
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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
- cortex
-
ache
- hippocampus
- forebrain
-
neurotransmitter
-
medial
-
innervation
- alzheimer
- cortical
-
muscarinic
-
neurochemical
- striatum
- axon
- spinal
-
maze
-
basalis
- septal
-
neurotrophic
-
ventral
-
retrograde
- ganglion
- ngf
-
presynaptic
-
parasympathetic
- myenteric
-
afferent
-
varicosity
-
chat-positive
- motoneuron
-
interneurons
-
gabaergic
- tegmental
-
diagonal
- meynert
-
magnocellularis
-
ibotenic
- medicine
-
wga-hrp
-
calretinin
-
ache-positive
- diagnostics
- broca
- benzilate
-
pedunculopontine
-
non-cholinergic
- analysis
-
intermediolateral
-
amacrine
- pharmacology
-
preganglionic
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyl CoA:choline-O-acetyltransferase
-
-
-
-
acetyl-CoA:choline-O-acetyltransferase
-
-
-
-
acetyltransferase, choline
-
-
-
-
cChAT
chAcT
-
-
-
-
ChAT
choline acetyl transferase
-
-
-
-
choline acetylase
-
-
-
-
choline acetyltransferase
pChAT
ChAT
-
-
choline acetyltransferase
-
-
-
-
choline acetyltransferase
-
-
pChAT
-
peripheral choline O-acetyltransferase, predominantly found in peripheral neurons
pChAT
-
peripheral choline O-acetyltransferase, predominantly found in peripheral neurons
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + choline = CoA + O-acetylcholine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:choline O-acetyltransferase
Propanoyl-CoA can act, more slowly, in place of acetyl-CoA.
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CAS REGISTRY NUMBER
COMMENTARY
9012-78-6
-
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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
additional information
?
-
-
pilocarpine-induced seizures produce alterations on choline acetyltransferase and acetylcholinesterase activities and deficit memory in rats, overview
-
-
?
acetyl-CoA + carnitine
acetylcarnitine + CoA
-
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
-
-
-
-
?
acetyl-CoA + choline
acetylcholine + CoA
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
-
-
-
-
?
acetyl-CoA + choline
acetylcholine + CoA
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
-
-
-
-
?
acetyl-CoA + choline
acetylcholine + CoA
-
-
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
-
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
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
-
synthesis of the neurotransmitter acetylcholine, deficiency in ChAT involved in several neurological and psychiatric disorders
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
-
-
487277, 487278, 487285, 487288, 487295, 487297, 487301, 487305, 487310, 487316, 487318, 487322, 487323, 487324, 487329, 487330, 487331
-
-
?
acetyl-CoA + choline
acetylcholine + CoA
-
-
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
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
synthesis of the neurotransmitter acetylcholine, mutations in ChAT causes congenital neuromuscular disorders
-
-
r
acetyl-CoA + choline
CoA + O-acetylcholine
-
-
acetylcholine is the primary parasympathetic neurotransmitter in the airways
-
?
acetyl-CoA + choline
CoA + O-acetylcholine
-
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
-
?
acetyl-CoA + choline
CoA + O-acetylcholine
-
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
-
-
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
-
pilocarpine-induced seizures produce alterations on choline acetyltransferase and acetylcholinesterase activities and deficit memory in rats, overview
-
-
?
acetyl-CoA + choline
acetylcholine + CoA
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
-
synthesis of the neurotransmitter acetylcholine, deficiency in ChAT involved in several neurological and psychiatric disorders
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
-
synthesis of the neurotransmitter acetylcholine
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
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
synthesis of the neurotransmitter acetylcholine, mutations in ChAT causes congenital neuromuscular disorders
-
-
r
acetyl-CoA + choline
CoA + O-acetylcholine
-
-
acetylcholine is the primary parasympathetic neurotransmitter in the airways
-
?
acetyl-CoA + choline
CoA + O-acetylcholine
-
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
-
?
acetyl-CoA + choline
CoA + O-acetylcholine
-
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
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
additional information
additional information
metal binding site found in crystal structure analysis, bound metal is most likely a Na+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-(azepan-1-yl)-3-[(8-ethyl-4a,5-dihydro-4H-[1,2,4]triazino[5,6-b]indol-3-yl)sulfanyl]propan-1-one
the amide carbonyl of the compound forms a hydrogen bond with the Ser540 amino acid residue of ChAT with a distance of 2.15 A. The 5H-[1,2,4]triazino[5,6-b]indole nucleus forms a hydrogen bond with the Gly329 amino acid residue of ChAT active site
1-[2-[(naphthalen-1-yl)amino]-1,3-thiazole-4-carbonyl]-N-(propan-2-yl)piperidine-4-carboxamide
the terminal amide carbonyl forms a hydrogen bond with Ser438 at a distance of 1.88 A, while the thiazole nucleus forms pi_pi interactions with the Tyr436 amino acid residue of the active site of ChAT
2-(alpha-naphthoyl) ethyltrimethylammonium iodide
i.e. alpha-NETA, commercially available inhibitor. The naphthyl group forms pi-pi interaction with residue Tyr552, while the quaternary trimethyl ammonium moiety is closely surrounded by His324, Pro98, Asp328 residues. The naphthyl moiety is accommodated in a pocket consisting of Asn95, Pro554, Gly553, Thr539, and Ser538 residues. The determined IC50 values are 34.18 microM for acetylcholinesterase and 33.30 microM for butanoylcholinesterase
2-[[5-(furan-2-yl)-1H-1,2,4-triazol-3-yl]sulfanyl]-1-[4-(propan-2-yl)phenyl]ethan-1-one
compound makes the His324 residue inaccessible for the catalysis
amyloid beta peptide
-
the aggregated form of A-beta 25-35 decreased significantly enzyme activity only in the aged striatum
-
Flubenzimine
-
i.e. N-[3-phenyl-4,5-bis[(trifluoromethyl)immino]-2-thiazolidinylidene]benzenamine
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
nerve growth factor
-
nerve growth factor, under specific development conditions, leads to a paradoxical down-regulation of the enzyme
-
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
N-ethylmaleimide
-
the enzyme is completely protected against N-ethylmaleimide inactivation by acetyl coenzyme A and is substantially protected by acetyl choline
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
additional information
design of ChAT ligands based on molecular docking, Hologram Quantitative Structure Activity Relationship (HQSAR) and lead optimization. The Tyr552 and His324 amino acid residues are of outmost importance for stabilization of an active conformation of ligands of ChAT
-
additional information
identification of inhibitors by hierarchical virtual screening approach on a commercial library of about 300,000 compounds, followed by in vitro screening of the hits by a high-throughput ChAT assay
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
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
-
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
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
Cl-
-
enzyme activity increases in the presence of ionic strength, Cl- is the most potent activator in comparison with Br-and I-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
Oenanthe siolonifera
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
Sasamorpha purpurascens
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
ethanolic extract of Allium tuberosum
-
activates choline acetyltransferase. It is suggested that ferulic acid from Allium tuberosum Rottl. is the strong ChAT activator
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
dependence on salt concentration
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.007
1-(azepan-1-yl)-3-[(8-ethyl-4a,5-dihydro-4H-[1,2,4]triazino[5,6-b]indol-3-yl)sulfanyl]propan-1-one
Homo sapiens
pH 7.4, 37°C
0.0165
1-[2-[(naphthalen-1-yl)amino]-1,3-thiazole-4-carbonyl]-N-(propan-2-yl)piperidine-4-carboxamide
Homo sapiens
pH 7.4, 37°C
0.0254
2-[[5-(furan-2-yl)-1H-1,2,4-triazol-3-yl]sulfanyl]-1-[4-(propan-2-yl)phenyl]ethan-1-one
Homo sapiens
pH 7.4, 37°C
0.0025
Hg2+
Electrophorus electricus
-
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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
73
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
additional information
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
zebrafish mutant line, bajan, in which compromised motility and fatigue result from a point mutation in the gene coding choline acetyltransferase
Uniprot
brenda
-
487277, 487278, 487279, 487290, 487294, 487300, 487302, 487303, 487313, 487315, 487320, 487330, 658358, 660442
-
-
brenda
-
487277, 487278, 487279, 487285, 487288, 487295, 487297, 487301, 487305, 487310, 487316, 487318, 487322, 487323, 487324, 487328, 487329, 487330, 487331, 657464
-
-
brenda
-
-
-
brenda
two splicing variants, peripheral-type pChAT and common-type cChAT
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
developing antenna during larvae development, enzyme detected in neurons, glia and epidermal cells
brenda
-
pChAT+ nerve fibers are found exclusively in the trigeminal and solitary systems. The ventral portion of the principal sensory nucleus contains many pChAT+ fibers
brenda
-
ChAT activity is higher in Ts65Dn mice at both 19 and 24 months of age compared to normogenic animals
brenda
-
impaired spatial working memory and altered choline acetyltransferase immunoreactivity and nicotinic receptor binding in rats exposed to intermittent hypoxia during sleep
brenda
-
afferent varicose fibers are immunopositive for ChAT in the ventral telencephalon, the preoptic area, the hypothalamus and the posterior tuberculum
brenda
-
strong pChAT signal in intrinsic primary afferent neurons, low immunoreactivity for cChAT
brenda
-
no significant differences of ChAT activity are measured at both 19 and 24 months of age between Ts65Dn mice and normogenic animals
brenda
-
no significant differences of ChAT activity are measured at both 19 and 24 months of age between Ts65Dn mice and normogenic animals
brenda
-
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
brenda
-
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
brenda
-
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
brenda
-
afferent varicose fibers are immunopositive for ChAT in the ventral telencephalon, the preoptic area, the hypothalamus and the posterior tuberculum
brenda
-
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
brenda
-
afferent varicose fibers are immunopositive for ChAT in the ventral telencephalon, the preoptic area, the hypothalamus and the posterior tuberculum
brenda
-
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
brenda
-
afferent varicose fibers are immunopositive for ChAT in the ventral telencephalon, the preoptic area, the hypothalamus and the posterior tuberculum
brenda
-
pChAT occurs in most CGRP+ SP+ ganglion cells, such sparseness of pChAT+ fibers implies poor transportation of pChAT to axon branchlets
brenda
-
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
brenda
additional information
-
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
brenda
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ChAT immunopositive neurons are present in several nuclei of the forebrain, the midbrain, the hindbrain and the spinal cord
brenda
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silencing of choline acetyltransferase expression by lentivirus-mediated RNA interference
brenda
-
-
brenda
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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
brenda
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silencing of choline acetyltransferase expression by lentivirus-mediated RNA interference
brenda
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increased ChAT activity in some brain regions, notably the hippocampus, of patients diagnosed with mild cognitive impairment
brenda
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ChAT activity is increased at 10 and 12 months of age in the hippocampus of Ts65Dn mice compared to normogenic animals
brenda
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cholinergic neuron-specific ChAT in the CA1 region of hippocampus
brenda
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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
brenda
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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
brenda
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ChAt activity in untreated and in pilocarpine-treated hippocampi, overview
brenda
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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
brenda
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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
brenda
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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
brenda
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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
brenda
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silencing of choline acetyltransferase expression by lentivirus-mediated RNA interference
brenda
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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
brenda
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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
brenda
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ChAT immunopositive neurons are present in several nuclei of the forebrain, the midbrain, the hindbrain and the spinal cord
brenda
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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
brenda
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only a few ChATir neurons are found outside the somatomotor groups in the ventral gray
brenda
additional information
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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
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
associated with synaptic vesicles, can be displaced by treatment with urea or alkaline solutions
brenda
additional information
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immunofluorescent localization study, overview
-
brenda
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cChAT but not pChAT, pChAT found in nucleus only after treatment with leptomycin B
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
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
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
-
loss of enzyme activity is associated with dementia with Lewy bodies
malfunction
the reduction in levels of O-acetylcholine is one of the most significant physiological symptoms of Alzheimer's disease
physiological function
-
acetylcholine, synthesized by ChAT, and muscarinic M1, M2, and M3 receptors are involved in fibroblast proliferation
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
peripheral type of choline acetyltransferase-positive nerves participate in the sympathetic cholinergic innervation of eccrine sweat glands. The enzyme also plays a role in cutaneous sensory nerve endings
physiological function
soluble cerebrospinal fluid enzyme levels show strong correlation with soluble complement factor levels, supporting a role in inflammatory regulation
physiological function
acute exposure to amyloid Abeta1-42 results in increased association of ChAT with chromatin and formation of ChAT aggregates in nuclei. Abeta1-42 -exposure increases ChAT association with gene promoters and introns. The Abeta1-42 -induced ChAT aggregates colocalize with special AT-rich binding protein 1 (SATB1), which anchors DNA to scaffolding/matrix attachment regions (S/MARs). Both ChAT and SATB proteins associate with synapse and cell stress genes. After Abeta1-42 -exposure, both SATB1 and ChAT are enriched at the same S/MAR on the APP gene, with ChAT expression attenuating an increase in an isoform-specific APP mRNA transcript
physiological function
both soluble amyloid Abeta40 and Abeta42 enhance the catalytic efficiency of ChAT byabout 21% and 26% at physiological concentration ranges found in cerebrospinal fluid. Activation of ChAT by Abeta is highly specific. Abeta42 exhibits an EC50 of activation at 10fold lower concentrations compared to Abeta40. The activation is persistent even in the presence of a physiological Abeta40/42 mixture ratio, expected in human cerebrospinal fluid
physiological function
choline acetyltransferase is robustly induced in both CD4+ and CD8+ T cells during lymphocytic choriomeningitis virus infection in an IL-21-dependent manner. Deletion of ChAT within the T cell compartment in mice ablates vasodilation in response to infection, impairs the migration of antiviral T cells into infected tissues, and ultimately compromises the control of chronic lymphocytic choriomeningitis virus clone 13 infection
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
enzyme interacts with heat shock proteins HSC/HSP70 and HSP90. Inhibition of heat shock proteins reduces cellular ChAT activity and solubility, and enhances the ubiquitination and proteasome-dependent loss of ChAT protein. The effects of HSP inhibition are greater for mutant ChAT proteins P17A/P19A and congenital myasthenic syndrome-related mutants V18M and A513T compared to wild-type ChAT. siRNA-mediated knock-down of E3 ubiquitin ligase CHIP has no effect on either wild-type or mutant ChAT protein levels. Inhibition of the endoplasmic reticulum and heat shock protein-associated cochaperone p97/VCP prevents degradation of ubiquitinated ChAT
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
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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_CAEEL
627
0
71317
Swiss-Prot
other Location (Reliability: 1)
CLAT_CHICK
640
0
72623
Swiss-Prot
other Location (Reliability: 1)
CLAT_DANRE
637
0
71840
Swiss-Prot
other Location (Reliability: 2)
CLAT_DROME
721
0
81328
Swiss-Prot
other Location (Reliability: 3)
CLAT_HUMAN
748
0
82536
Swiss-Prot
other Location (Reliability: 3)
CLAT_MOUSE
641
0
71853
Swiss-Prot
other Location (Reliability: 2)
CLAT_PIG
641
0
71731
Swiss-Prot
other Location (Reliability: 1)
CLAT_RAT
640
0
71864
Swiss-Prot
other Location (Reliability: 2)
B7PRX0_IXOSC
316
0
35312
TrEMBL
other Location (Reliability: 1)
B7QAT6_IXOSC
86
0
9863
TrEMBL
other Location (Reliability: 3)
B7PGR3_IXOSC
527
0
60076
TrEMBL
other Location (Reliability: 2)
B7PWG8_IXOSC
256
0
28723
TrEMBL
other Location (Reliability: 2)
B7QD11_IXOSC
618
0
68743
TrEMBL
other Location (Reliability: 4)
B7PN81_IXOSC
219
0
24864
TrEMBL
other Location (Reliability: 5)
B7QNL9_IXOSC
151
0
17232
TrEMBL
other Location (Reliability: 3)
B7PAZ5_IXOSC
407
0
45099
TrEMBL
other Location (Reliability: 2)
A0A6J8C1N5_MYTCO
658
0
75394
TrEMBL
other Location (Reliability: 2)
B7PGB4_IXOSC
144
0
16342
TrEMBL
other Location (Reliability: 3)
Q6LEN6_HUMAN
138
0
15355
TrEMBL
other Location (Reliability: 2)
B7PVQ2_IXOSC
231
0
26175
TrEMBL
other Location (Reliability: 1)
B7Q2W7_IXOSC
316
0
35025
TrEMBL
other Location (Reliability: 4)
E0VY59_PEDHC
650
0
74164
TrEMBL
Mitochondrion (Reliability: 5)
B7PPG9_IXOSC
247
0
27779
TrEMBL
other Location (Reliability: 2)
B7QCG6_IXOSC
191
0
21298
TrEMBL
other Location (Reliability: 2)
B7PTD1_IXOSC
281
0
31602
TrEMBL
other Location (Reliability: 5)
E0W162_PEDHC
650
0
74130
TrEMBL
other Location (Reliability: 1)
Q6LEN5_HUMAN
34
0
3724
TrEMBL
other Location (Reliability: 2)
Q6LBL1_HUMAN
17
0
1768
TrEMBL
other Location (Reliability: 1)
B7QNL8_IXOSC
149
0
16314
TrEMBL
other Location (Reliability: 2)
A0A0G3VI27_CHISP
236
0
26712
TrEMBL
other Location (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
106000
-
largest aggregate, formation after ammonium sulfate fractionation, gel filtration
13000
-
1 * 54000 + 1 * 13000, major form isolated, may be generated from monomeric form by limited proteolysis, SDS-PAGE
30000 - 300000
-
self-association to large aggregates, gel filtration, sedimentation equilibrium
34000
37000
-
x * 37000 + x * 56000, SDS-PAGE, ultracentrifugation in presence of guanidine-HCl
54000
56000
-
x * 37000 + x * 56000, SDS-PAGE, ultracentrifugation in presence of guanidine-HCl
62000
65000
66000
67000
67000 - 69000
68000
69000
76000
additional information
54000
-
1 * 54000 + 1 * 13000, major form isolated, may be generated from monomeric form by limited proteolysis, SDS-PAGE
67000 - 69000
-
gel filtration, sucrose density gradient centrifugation
68000
-
1 * 68000, enzyme is initially synthesized as 75 kDa precursor-protein, SDS-PAGE
68000
-
1 * 68000, enzyme is initially synthesized as 75 kDa precursor-protein, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
?
-
x * 37000 + x * 56000, SDS-PAGE, ultracentrifugation in presence of guanidine-HCl
dimer
-
1 * 54000 + 1 * 13000, major form isolated, may be generated from monomeric form by limited proteolysis, SDS-PAGE
monomer
-
1 * 68000, enzyme is initially synthesized as 75 kDa precursor-protein, SDS-PAGE
monomer
-
gel filtration, dimerization caused by oxidation can be reversed by addition of reducing agents
monomer
-
1 * 68000, enzyme is initially synthesized as 75 kDa precursor-protein, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
-
serine 440 of the recombinant human 69-kDa protein is the phoshorylation site
phosphoprotein
-
rat choline acetyltransferase is phosphorylated in Sf9 cells
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
additional information
-
increasing ionic strength increases susceptibility to thermal degradation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
bovine serum albumin stabilizes
EDTA stabilizes
increasing ionic strength increases susceptibility to proteolysis and thermal degradation
-
sucrose stabilizes
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
extremely sensitive to oxidation due to its cysteine-rich nature, oxidation causes formation of dimers and loss of activity
-
660442
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, partially purified preparation, several months stable, less stable in purified state
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2 isozymes
overview procedures
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNAs encoding splicing variants cChAT and pChAT, purified from the rat striatum and pterygopalatine ganglion, respectively, expression analysis. Recombinant expression in HEK-293 cells
-
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 using a baculovirus expression system
-
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
-
residues 18-617 of full length DNA expressed in Escherichia coli DH5alphaF’IQ
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
-
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
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cerebral spinal fluid enzyme is upregulated in autoimmune neuroinflammation
enzyme activity is reduced significantly when neurons are exposed to high levels of beta-amyloid aggregates
Nelumbo nucifera semen extract improves memory in rats with scopolamine-induced amnesia through the induction of choline acetyltransferase expression
-
the administration of 0.5% gamma-aminobutyric acid in the diet of ovariectomized female rats causes an increase in the activity of choline acetyltransferase in the brain
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APPLICATION
ORGANISM
UNIPROT
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
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
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
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
medicine
-
ChAT 2384 A allele is a risk factor for Alzheimer’s disease and mild cognitive impairment
medicine
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
-
promoting ChAT activity and acetylcholine release can lead to treatments for neurodegenerative diseases with cholinergic deficits, such as Alzheimer’s disease
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