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. Author manuscript; available in PMC: 2022 Jul 13.
Published in final edited form as: Nat Struct Mol Biol. 2021 Aug 11;28(8):662–670. doi: 10.1038/s41594-021-00633-2

Extended Data Fig. 6 |. FLCN-10 peptide uncompetitively inhibits LDHA.

Extended Data Fig. 6 |

a) Michaelis-Menten kinetics of LDHA in the presence of FLCN protein, FLCN-10 peptide, or FX11 (n=3). Data shown as mean ± s.d. b) FLCN-10 is an uncompetitive inhibitor of LDHA based on Lineweaver-Burke plot (n=3). c–e) IC50 measurements for LDHA in the presence of FLCN protein, FLCN-10 peptide, or FX-11 (n=3). Data shown as mean ± s.d. f) Summary of LDHA enzyme kinetics. g) LDHA-R106-FLAG mutants were transiently transfected and immunoprecipitated from HEK293 cells. FLCN interaction assessed by immunoblotting. Binding to FLCN-10-Biotin peptide was assessed by Streptavidin pulldown.