. Author manuscript; available in PMC: 2012 Jun 28.

Published in final edited form as: Biochemistry. 2011 Jun 6;50(25):5767–5779. doi: 10.1021/bi2005416

Table 2.

The Yields of the Products from the Reaction of GAP in D₂O in the Presence of Triosephosphate Isomerase from Different Organisms.^a

[TIM]		Fractional Product Yield
[TIM]		DHAP	d-DHAP	d-GAP	MG
T brucei	f_T^b	0.42^c	0.35^c	0.22^c	0.01^c
	f_T^b	0.36^d	0.37^d	0.21^d	0.06^d
	f_E^e,^f	0.40± 0.02	0.37 ± 0.02	0.22 ± 0.002

T. brucei (monoTIM)	f_T^b	0.31^g	0.34^g	0.32^g	0.03^g
	f_T^b	0.33^h	0.33^h	0.26^h	0.09^h

	f_E^e, ^f	0.34 ± 0.02	0.35 ± 0.01	0.31 ± 0.02

Rabbit Muscle (50)	f_E^e	0.49	0.31	0.20

Chicken Muscle (50)	f_E^e	0.50	0.31	0.19

For the reaction of GAP at pD 8.0 (15 mM imidazole), 25 °C and I = 0.1 (NaCl).

Yield of the product of the enzymatic or nonenzymatic reactions of GAP (Scheme 2) determined by extrapolation to zero time of linear plots of product yield against time (data not shown).

Reaction of 10 mM GAP catalyzed by 0.60 nM TIM (Figure 1).

Reaction of 5 mM GAP catalyzed by 0.3 nM TIM (data not shown).

Normalized yields of the products of TIM-catalyzed reactions, calculated using eq 4–6 (Figure 1).

The quoted errors are the average of product yields determined in two reactions catalyzed by 0.3 nM or 0.6 nM Tbb TIM.

Reaction of 10 mM GAP catalyzed by 660 nM monoTIM in D₂O (I = 0.1, NaCl).

Reaction of 19 mM GAP catalyzed by 600 nM monoTIM in D₂O (I = 0.06).