Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Chemical Compound Review:

AC1L1947 [5-(6-aminopurin-9-yl)-4- hydroxy-2...

Synonyms:

Czuba, B. et al., Kelley, M. et al., Sfakianos, M.K. et al., Czuba, B. et al.

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High impact information on Choloyl-CoA

However, preincubation of wild-type hBAT with the substrate cholyl-CoA before NEM treatment prevented loss of N-acyltransferase activity [1].
The reaction of cholic acid, CoA and ATP to yield cholyl-CoA was investigated by kinetic analysis of the reaction as catalysed by guinea pig liver microsomes [2].
Purification and characterization of cholyl-CoA: taurine N-acetyltransferase from the liver of domestic fowl (Gallus gallus) [3].
Unlike the N-acyltransferase from five other mammalian species, the enzyme from dog liver was unable to synthesize glycine conjugates from cholyl-CoA in vitro even in the presence of 0.1 M glycine [4].

References

Conserved residues in the putative catalytic triad of human bile acid Coenzyme A:amino acid N-acyltransferase. Sfakianos, M.K., Wilson, L., Sakalian, M., Falany, C.N., Barnes, S. J. Biol. Chem. (2002) [Pubmed]
Determination of the mechanism of reaction for bile acid: CoA ligase. Kelley, M., Vessey, D.A. Biochem. J. (1994) [Pubmed]
Purification and characterization of cholyl-CoA: taurine N-acetyltransferase from the liver of domestic fowl (Gallus gallus). Czuba, B., Vessey, D.A. Biochem. J. (1981) [Pubmed]
Identification of a unique mammalian species of cholyl-CoA: amino acid N-acyltransferase. Czuba, B., Vessey, D.A. Biochim. Biophys. Acta (1981) [Pubmed]

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