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. 2021 Nov 15;60(47):3621–3632. doi: 10.1021/acs.biochem.1c00672

Table 3. Inhibition Patterns and Constants by the l-Met Analogue l-cLeua.

variable substrate fixed substrate inhibition pattern inhibition constant (μM)
l-Met saturating ATP C Kis = 290 ± 30
l-Met nonsaturating ATP C Kis = 160 ± 20
ATP saturating l-Met NI ND
ATP nonsaturating l-Met U Kii = 510 ± 20
a

At pH 7.5 and 22 °C. Saturating ATP = 1 mM, Nonsaturating ATP = 0.07 mM, saturating l-Met = 0.6 mM, and nonsaturating l-Met = 0.02 mM. C indicates competitive inhibition, NI indicates no inhibition, and U indicates uncompetitive inhibition.