10-formyltetrahydrofolate dehydrogenase, ALDH family 1L
10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Feature 1:NADP binding site [chemical binding site]
Evidence:
Structure:2O2Q: rat 10'formyltetrahydrofolate dehydrogenase in complex with NADP+, defined using 3.5 A. - View structure with Cn3D
Structure:2O2R: rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH, defined using 3.5 A. - View structure with Cn3D
Comment:FTHFDH binds the 2'-phosphate group of NADP via a water-mediated contact with Gln600 that may contribute to the specificity of the enzyme for NADP over NAD.
Comment:When reduced, the nicotinamide ring of NADP is displaced from the active site, restoring the contact between Cys707 and Glu673 and allowing the latter to activate the hydrolytic water molecule in deacylation.
Jiyao W et al.(2023). "The conserved domain database in 2023.",