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Article

Deficient synthesis of MTHFD, a trifunctional folate-dependent enzyme, in the CHO Ade E mutant.

Somatic cell and molecular genetics - 1 Jul 1991

Mascisch A, Rozen R

Abstract excerpt

MTHFD is a folate-dependent trifunctional protein comprised of three activities: N5,N10-methylenetetrahydrofolate dehydrogenase, N5,N10-methenyltetrahydrofolate cyclohydrolase, and N10-formyltetrahydrofolate synthetase. The enzymes catalyze sequential interconversion of tetrahydrofolate derivatives required for purine, methionine, and thymidylate synthesis. A Chinese hamster ovary cell line (Ade-E), reported to...

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Identifiers

PMID: 1887335
DOI: 10.1007/BF01233064

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Deficient synthesis of MTHFD, a trifunctional folate-dependent enzyme, in the CHO Ade E mutant.PMID 1887335Read ↗

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Human mutations in methylenetetrahydrofolate dehydrogenase 1 impair nuclear de novo thymidylate biosynthesis.Semantic proximity Read ↗

Biochemical analysis of patients with mutations in MTHFD1 and a diagnosis of methylenetetrahydrofolate dehydrogenase 1 deficiency.Semantic proximity Read ↗

NAD- and NADP-dependent mitochondrially targeted methylenetetrahydrofolate dehydrogenase-cyclohydrolases can rescue mthfd2 null fibroblasts.Semantic proximity Read ↗

The N-terminal, dehydrogenase/cyclohydrolase domain of yeast cytoplasmic trifunctional C1-tetrahydrofolate synthase requires the C-terminal, synthetase domain for the catalytic activity in vitro.Semantic proximity Read ↗

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