. Author manuscript; available in PMC: 2014 Oct 29.

Published in final edited form as: Biochemistry. 2013 Oct 15;52(43):7678–7688. doi: 10.1021/bi400962r

Table 3.

Kinetic data for PR-catalyzed hydrolysis of synthetic peptides corresponding to natural cleavage sites in HIV-1 Gag polyprotein

Substrate	Sequence	Enzyme	K_m (mM)	k_cat (s⁻¹)	k_cat/K_m (mM⁻¹s⁻¹)	Activty (%) relative to PR	Order of cleavage^a
MA/CA	VSQNY↓PIVQ	PR	0.15	6.9	46.0		2
		PR20	0.91	3.0	3.2	7	1
CA/SP1	KARVL↓AEAMS	PR	0.02	0.9	42.4^b		3
		PR20	0.11	0.1	1.2	2.8	3
SP1/NC	TATIM↓MQRGN	PR	0.10	6.7	67.0		1
		PR20	0.10	0.2	2.0	3.0	2
NC/SP2	ERQAN↓FLGKI	PR	0.17	0.15	0.9^c		5
		PR20	0.23	0.0005	0.002	0.2	6
NC/SP2 mutant	ERRVN↓FLGKI	PR	nd	nd	20.1^c		4
		PR20	0.23	0.01	0.04	0.2	4
SP2/p6	RPQNF↓LQSRP	PR	0.48	0.4	0.8		6
		PR20	0.43	0.01	0.02	2.5	5

Relative efficiency for cleavage of each substrate by the same enzyme, from highest (1) to lowest (6)

reference⁴⁰

reference³⁹