. Author manuscript; available in PMC: 2020 Jun 4.

Published in final edited form as: Biochemistry. 2018 Nov 15;57(48):6726–6734. doi: 10.1021/acs.biochem.8b00889

Table 1:

Steady State Parameters for 15-LOX-1 and 12-LOX reaction with 5,15-diHpETE and 5,15-diHETE

Enzyme	Substrate	k_cat (s⁻¹)	K_m (µM)	k_cat/K_m(µM⁻¹s⁻¹)
12-LOX	AA (_{C10 abstraction})	18 ± 0.8	1.0 ± 0.1	18±2
15-LOX-1	AA (_{C10 abstraction})	1.4 ± 0.1^*	6 ± 1	0.23 ± 0.03^*

12-LOX	5,15-diHpETE	0.17 ± 0.007	14 ± 1	0.011 ± 0.007
15-LOX-1	5,15-diHpETE	4.6 + 0.1	23 ± 2	0.21 ± 0.01

12-LOX	5,15-diHETE^**	0.18 ± 0.02	113 ± 19	0.0015 ± 0.0001
15-LOX-1	5,15-diHETE^**	nr^***	nr	nr

k_cat and k_cat/K_m values were confirmed daily relative to the k_cat and k_cat/K_m values of AA. The C10 abstraction kinetic values of 15-LOX-1 are 10% of the AA kinetic values, which include both the 15-HpETE and 12-HpETE kinetics (k_cat and k_cat/K_m for AA are 14 ± 1s⁻¹ and 2.3 ± 0.3µM⁻¹ s⁻¹, respectively)

^**

3µM of 13-HPODE is added to activate 12-LOX.

^***

nr = no reaction