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. 1977 Aug 1;165(2):321–326. doi: 10.1042/bj1650321

Acetyl-coenzyme A and coenzyme A analogues. Their effects on rat brain choline acetyltransferase.

J Rossier
PMCID: PMC1164904  PMID: 921752

Abstract

Choline acetyltransferase has the same affinity for acetyl-CoA, propionyl-CoA and butyryl-CoA (Km=1.4 micron). Choline acetyltransferase may use the two latter compounds as substrate, but the longer the acyl chain the lower will be Vmax. CoA is an inhibitor (Ki=1.8 micron). The position of the 3'-phosphate is of primary importance. Desphospho-CoA is a weak inhibitor (Ki=500 micron). 5'-AMP is already an inhibitor (Ki=2500 micron). Phosphopantetheine is not an inhibitor. Dextran Blue is a potent inhibitor (Ki=0.05 micron). Choline acetyltransferase binds to hydrophobic affinity columns. Because of its affinity for nucleotides, affinity for Dextran Blue and hydrophobicity, it is proposed that it contains the 'nucleotide fold', which is a common structural domain present in several enzymes binding nucleotides.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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