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. 2010 Nov;19(11):2031–2044. doi: 10.1002/pro.505

Table II.

Biochemical and Biological Impacts of Dominant-Negative Heterozygous Mutations (H391Y, K422R)(37,38)

S. no. Features Wild PKM2 H391Y K422R
1 Enzymatic activity 100% 80% 25%
2 PEP affinity Normal Increased by sixfold Reduced by threefold
3 Catalytic efficiency Normal Increased Reduced
4 Oligomeric state Homotetramer Homotetramer Homotetramer
5 Cooperativity Allosteric Completely lost Increased
6 Activation by FBP Yes No Yes
7 Optimum pH 7.4 7.0 7.0
8 Thermostability No Yes No
9 α Helical content Rich Increased Increased
10 Structural rigidity Absent Present Absent

When coexpressed with PK-WT in in vitro transfection assays

11 Cross-monomer interaction Yes Yes Yes
12 Oligomeric state Normal Disturbed Disturbed
13 Heterooligomerization Yes Yes Yes
14 Heterodimerization No Yes Yes
15 Enzymatic activity Unaffected Reduced Reduced
16 PEP affinity Unaffected Reduced Reduced
17 E. coli doubling time Slightly reduced Reduced Reduced
18 Rate of cell division Slightly increased Promoted Promoted
19 Polyploidy Unaffected Promoted Promoted