Literature summary for 2.3.1.6 extracted from

Kim, A.R.; Doherty-Kirby, A.; Lajoie, G.; Rylett, R.J.; Shilton, B.H.
Two methods for large-scale purification of recombinant human choline acetyltransferase (2005), Protein Expr. Purif., 40, 107-117.

Search for more literature for 2.3.1.6

Cloned(Commentary)

Cloned (Comment)	Organism
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	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
acetyl-CoA + choline	Homo sapiens	synthesis of the neurotransmitter acetylcholine, deficiency in ChAT involved in several neurological and psychiatric disorders	acetylcholine + CoA	-	r

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Oxidation Stability

Oxidation Stability	Organism
extremely sensitive to oxidation due to its cysteine-rich nature, oxidation causes formation of dimers and loss of activity	Homo sapiens

Purification (Commentary)

Purification (Comment)	Organism
recombinant proteins using His-tag or chitin-binding-domain	Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
brain	-	Homo sapiens	-
placenta	-	Homo sapiens	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
50	-	purified enzyme, pH 7.4	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acetyl-CoA + choline	-	Homo sapiens	acetylcholine + CoA	-	r
acetyl-CoA + choline	synthesis of the neurotransmitter acetylcholine, deficiency in ChAT involved in several neurological and psychiatric disorders	Homo sapiens	acetylcholine + CoA	-	r

Subunits

Subunits	Comment	Organism
monomer	gel filtration, dimerization caused by oxidation can be reversed by addition of reducing agents	Homo sapiens

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Release 2023.1 (January 2023)