Table 1.

Summary of studies that evaluated the ability of human GLYAT to conjugate isovaleryl-CoA to glycine.

Enzyme preparation	CoA substrates evaluated	Amino acid substrates evaluated	Formation ofN-isovalerylglycine	Reference
Enzyme extract from human liver and kidney tissue	phenylacetyl-CoA benzoyl-CoA isobutyryl-CoA isovaleryl-CoA indolyl acetyl-CoA p-hydroxyphenylacetyl-CoA	glycine glutamine	No	[41]
Human liver lysate	2-methyl butyryl-CoA isobutyryl-CoA butyryl-CoA hexanoyl-CoA octanoyl-CoA decanoyl-CoA isovaleryl-CoA	glycine	N-isovalerylglycine formed under experimental conditions not comparable to physiological conditions	[42]
Enzyme preparation isolated from human liver	benzoyl-CoA butyryl-CoA salicylyl-CoA heptanoyl-CoA isovaleryl-CoA	glycine	isovaleryl-CoA had the lowest substrate specificity	[43]