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Cooperative substrate binding was observed, and the kinetic data were fitted to a two-substrate Hill equation. The coding region of the GLYAT gene was found to be highly conserved and the rare 156Asn Ser,199Arg Cys variant negatively affected the relative enzyme activity. Even though the 156Asn Ser,199Arg Cys variant had a higher affinity for benzoyl-CoA (s0.5,benz = 61.2 µM), kcat was reduced to 9.8% of the most abundant haplotype 156Asn Ser (s0.5,benz = 96.6 µM), while the activity of 17Ser Thr,156Asn
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