Table 1.

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

Enzyme	Substrate	KM (µM)	Ki (µM)	kcat (s−1)	kcat/KM (M−1·s−1)
BsAcuC (2c)	LGKaca	83	‒	0.022	0.3·103
	LGKproa	~160	‒	0.04	~0.2·103
	LGKcra	~170	‒	0.02	~0.1·103
KpHdaH (1b)	QPKKac	18	‒	0.057	3.1·103
LcApaH (3)	QPKKacb	~2000	~13	~123	~63·103
	QPKKpro	~300	‒	0.6	~2·103
	LGKaca	15.2	‒	2.10	139·103
	LGKproa	~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)	QPKKacb	~1000	~44	~74	~74·103
	QPKKpro	~200	‒	0.42	~2·103
	LGKaca	21	‒	1.56	75·103
	LGKproa	150	‒	0.065	0.43·103
PsApaH (4)	QPKKacb	43	122	0.09	2.1·103
RwDmhA (1b)	QPKKacb	42	154	0.024	0.6·103
VsHdaH (1b)	QPKKac	47	‒	1.73	37·103
	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.