Mutational and structural studies of (βα)₈-barrel fold methylene-tetrahydropterin reductases utilizing a common catalytic mechanism.

ABSTRACT: Methylene-tetrahydropterin reductases catalyze the reduction of a methylene to a methyl group bound to a reduced pterin as C₁ carrier in various one-carbon (C₁) metabolisms. F₄₂₀-dependent methylene-tetrahydromethanopterin (methylene-H₄MPT) reductase (Mer) and the flavin-independent methylene-tetrahydrofolate (methylene-H₄F) reductase (Mfr) use a ternary complex mechanism for the direct transfer of a hydride from F₄₂₀H₂ and NAD(P)H to the respective methylene group, whereas FAD-dependent methylene-H₄F reductase (MTHFR) uses FAD as prosthetic group and a ping-pong mechanism to catalyze the reduction of methylene-H₄F. A ternary complex structure and a thereof derived catalytic mechanism of MTHF

SUBMITTER: Gehl M 

PROVIDER: S-EPMC11094777 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature