The Role of Mitochondrial NADPH-Dependent Isocitrate Dehydrogenase in Cancer Cells

Table 1

Kinetics of IDH isoforms as compared to homodimeric mutant enzymes with clinically relevant mutations. Unless specified “reductive”, forward reactions were measured. “n.d.”: not determined.

Enzyme	Organism/tissue	Mutation	conditions	K𝑚 isocitrate (𝜇M)	K𝑙, 2-oxo-glutarate (𝜇M)	K𝑚 NADP^+ (𝜇M)	𝑉max (μmol·min^−1·mg^−1)	Reference
IDH1	Human	wt		65	1900	49	44000 s^−1	[96]
	Human	R132H		370	24	84	38 s^−1	[96]
	Human	R132H	Reductive	2OG: 965	n.d	NADPH: 0.44	1000 s^−1	[96]
	Human	wt		6.4	n.d.	n.d.	14	[101]
	Human	R132H		1280	n.d.	n.d.	0.8	[101]
	Rat liver	wt		120	n.d.	150	70	[102]
IDH2	Porcine	wt		8.4	n.d.	5.6	43	[103]
	Porcine	wt		6	n.d.	5	40	[51]
	Porcine	R133Q		990	n.d.	11	21	[51]
	Rat liver	wt		70	n.d.	60	66	[102]
	Rat heart	wt		45	80	46	16	[104]
	Rat heart	wt	Ischemic	17	250	46	38	[104]
IDH3	Human	wt	No ADP	2000	n.d.	NAD^+: 60	26	[105]
	Human	wt	+1 mM ADP	50	n.d.	n.d.	n.d.	[105]