Mitochondrial 10-formyltetrahydrofolate dehydrogenase

The N-terminal hydrolase domain has an NADP-independent formyltetrahydrofolate hydrolase activity, releasing formate and tetrahydrofolate.

The C-terminal aldehyde dehydrogenase domain has an NADP-dependent dehydrogenase activity. It catalyzes the oxidation of formate, released by the hydrolysis of formyltetrahydrofolate, into CO2.

The carrier domain is phosphopantetheinylated and uses the 4'-phosphopantetheine/4'-PP swinging arm to transfer the formyl group released by the N-terminal formyltetrahydrofolate hydrolase activity to the C-terminal aldehyde dehydrogenase domain that catalyzes its NADP-dependent oxidation into CO2 (PubMed:21238436). The overall NADP-dependent physiological reaction requires the 3 domains (N-terminal hydrolase, C-terminal aldehyde dehydrogenase and carrier domains) to convert formyltetrahydrofolate into tetrahydrofolate and CO2 (By similarity).

Mitochondrial 10-formyltetrahydrofolate dehydrogenase that catalyzes the NADP(+)-dependent conversion of 10-formyltetrahydrofolate to tetrahydrofolate and carbon dioxide.

Phosphopantetheinylation at Ser-375 by AASDHPPT is required for the formyltetrahydrofolate dehydrogenase activity.

In the N-terminal section; belongs to the GART family.

In the C-terminal section; belongs to the aldehyde dehydrogenase family. ALDH1L subfamily.

Highly expressed in pancreas, heart, brain and skeletal muscle.

• Mitochondrion

Mitochondrial 10-formyltetrahydrofolate dehydrogenase, Mitochondrial 10-FTHFDH, mtFDH, Aldehyde dehydrogenase family 1 member L2, ALDH1L2

• entrezGene:160428
• omim:613584
• swissprot:Q3SY69

Proteins

Metabolism

101746Da