Table 5.

Enzymatic and ligandin activities detected for Cys-GSTs.

		GSTL	DHAR	GHR	mPGES-2	GSTB	GSTO
Thiol-transferase		10–102abc	10–102a	102–103e	?	?	102–103egg
DHA reductase		10–102abc	103–104abd	10–102e	?	?	10–103egg
Glutathionylation		nd ac	nd a	nd e	?	10–103ij	nd–1 m
Deglutathionylation	PAP-SG	102–103c	?	nd e	?	?	103–104***ggn
	(Cl)Qui-SG	nd c	?	102–103ef	?	?	nd g
	TET-SG	nd c	?	?	?	?	103g
	Q-SG	1–102bc	?	?	?	?	?
PGH2 isomerization		?	?	?	102 * h	?	?
PGH2 degradation		?	?	?	103 ** h	?	?
Peroxidase		nd ac	nd a	nd e	?	0.1 k	nd m
Esterase		0.01–0.1 c	?	nd g	?	?	10 **** g
Ligandin		?	?	?		Antibiotics kl	Nitro-phenacyl glutathione o Tocopherol esters p

The data representing turnover numbers in min⁻¹ have been extracted from the following references:

^a(Dixon et al., 2002);

^b(Dixon and Edwards, 2010b);

^c(Lallement et al., 2014);

^d(Tang and Yang, 2013);

^e(Meux et al., 2011);

^f(Lam et al., 2012);

^g(Meux et al., 2013);

^h(Yamada and Takusagawa, 2007);

ⁱ(Allocati et al., 2000);

^j(Allocati et al., 2008);

^k(Perito et al., 1996);

^l(Allocati et al., 2009);

^m(Board et al., 2000);

ⁿ(Board and Anders, 2007);

^o(Brock et al., 2013);

^p(Sampayo-Reyes and Zakharyan, 2006).

Nd, not detected; ? not examined;

^*GSH-independent activity,

^**GSH-dependent activity,

^***a slightly different substrate, acetophenone, was used (Board and Anders, 2007),

^****k_cat/K_m in mM⁻¹.min⁻¹.