Table 1 Michaelis–Menten kinetics of deacylation of peptides by selected bacterial deacylases

Enzyme	Substrate	K_M (µM)	K_i (µM)	k_cat (s⁻¹)	k_cat/K_M (M⁻¹·s⁻¹)
BsAcuC (2c)	LGKac^a	83	‒	0.022	0.3·10³
	LGKpro^a	~160	‒	0.04	~0.2·10³
	LGKcr^a	~170	‒	0.02	~0.1·10³
KpHdaH (1b)	QPKKac	18	‒	0.057	3.1·10³
LcApaH (3)	QPKKac^b	~2000	~13	~123	~63·10³
	QPKKpro	~300	‒	0.6	~2·10³
	LGKac^a	15.2	‒	2.10	139·10³
	LGKpro^a	~280	‒	0.16	0.6·10³
	LGK(L-la)^a	170	‒	0.006	0.03·10³
	LGK(D-la)^a	62	‒	0.0022	0.04·10³
LpApaH (3)	QPKKac^b	~1000	~44	~74	~74·10³
	QPKKpro	~200	‒	0.42	~2·10³
	LGKac^a	21	‒	1.56	75·10³
	LGKpro^a	150	‒	0.065	0.43·10³
PsApaH (4)	QPKKac^b	43	122	0.09	2.1·10³
RwDmhA (1b)	QPKKac^b	42	154	0.024	0.6·10³
VsHdaH (1b)	QPKKac	47	‒	1.73	37·10³
VsHdaH (1b)	QPKK(L-la)	53	‒	0.044	0.8·10³

Shown are the enzymes, the peptide sequences with the acyl-modifications on the lysine side chains, and the results obtained for K_M, turnover number k_cat, and catalytic efficiency k_cat/K_M. The experiments were performed in two independent replicates (n = 2). Data are presented as means. Source data are provided as Source Data file.
^aData acquired with continuous assays.
^bData adjusted to enzyme kinetics with substrate inhibition at high concentration, with K_i as indicated.

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