in absence of KCl, 0.1 mM CoA inhibits activity over 40% irrespective of the concentration of glycine. In presence of KCl, CoA inhibits activity only slightly, less than 10%. In presence of potassium phosphate the inhibition is reduced to less than 2%. 2.5 mM, almost complete inhibition of salt-free enzyme
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molecular model containing coenzyme A. The inactivity of the R199C variant could be due to the substitution of the highly conserved Arg199 and destabilisation of an alpha-loop-alpha motif which is important for substrate binding
in a small cohort of South African Caucasian individuals, the two most prominent GLYAT haplotypes in all populations analysed, are S156 (70%) and T17S156 (20%). The S156C199 and S156H131 haplotypes, which have a negative effect on the enzyme activity of a recombinant human GLYAT, are detected at very low frequencies. An additional Q61L SNP occurring at a high frequency (12%) was detected
study to investigate 4-aminobenzoic acid as an alternative glycine conjugation probe. All of the participants were homozygous for increased enzyme activity, but excretion of product 4-amino-N-benzoylglycine varies significantly (16-56%, hippurate ratio)