ALDH1L1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2BW0, 2CFI, 2CQ8

Identifiers

Aliases

ALDH1L1, 10-FTHFDH, 10-fTHF, FDH, FTHFD, aldehyde dehydrogenase 1 family member L1

External IDs

MGI: 1340024 HomoloGene: 122031 GeneCards: ALDH1L1

Gene ontology
Molecular function	• formyltetrahydrofolate dehydrogenase activity • oxidoreductase activity • hydroxymethyl-, formyl- and related transferase activity • oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor • catalytic activity • 4-trimethylammoniobutyraldehyde dehydrogenase activity • aminobutyraldehyde dehydrogenase activity • aldehyde dehydrogenase (NAD) activity
Cellular component	• cytoplasm • extracellular exosome • mitochondrion • cytosol
Biological process	• metabolic process • one-carbon metabolic process • biosynthetic process • 10-formyltetrahydrofolate catabolic process • oxidation-reduction process • folic acid metabolic process
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


10840


107747

Ensembl


ENSG00000144908


ENSMUSG00000030088

UniProt


O75891


Q8R0Y6

RefSeq (mRNA)


NM_001270364 NM_001270365 NM_012190


NM_027406

RefSeq (protein)


NP_001257293.1 NP_001257294.1 NP_036322.2


NP_081682.1

Location (UCSC)

Chr 3: 126.1 – 126.2 Mb

Chr 6: 90.49 – 90.6 Mb

PubMed search

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Wikidata

View/Edit Human

View/Edit Mouse

10-formyltetrahydrofolate dehydrogenase is an enzyme that in humans is encoded by the ALDH1L1 gene.^[3]

The protein encoded by this gene catalyzes the conversion of 10-formyltetrahydrofolate, NADP, and water to tetrahydrofolate, NADPH, and carbon dioxide. The encoded protein belongs to the aldehyde dehydrogenase family and is responsible for formate oxidation in vivo. Deficiencies in this gene can result in an accumulation of formate and subsequent methanol poisoning.^[3]

References

Lee KM, Lan Q, Kricker A, et al. (2007). "One-carbon metabolism gene polymorphisms and risk of non-Hodgkin lymphoma in Australia.". Hum. Genet. 122 (5): 525–33. doi:10.1007/s00439-007-0431-2. PMID 17891500.
Stevens VL, McCullough ML, Pavluck AL, et al. (2007). "Association of polymorphisms in one-carbon metabolism genes and postmenopausal breast cancer incidence.". Cancer Epidemiol. Biomarkers Prev. 16 (6): 1140–7. doi:10.1158/1055-9965.EPI-06-1037. PMID 17548676.
Lim U, Wang SS, Hartge P, et al. (2007). "Gene-nutrient interactions among determinants of folate and one-carbon metabolism on the risk of non-Hodgkin lymphoma: NCI-SEER case-control study.". Blood. 109 (7): 3050–9. doi:10.1182/blood-2006-07-034330. PMC 1852210. PMID 17119116.
Oleinik NV, Krupenko SA (2004). "Ectopic expression of 10-formyltetrahydrofolate dehydrogenase in A549 cells induces G1 cell cycle arrest and apoptosis.". Mol. Cancer Res. 1 (8): 577–88. PMID 12805405.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Krupenko SA, Oleinik NV (2002). "10-formyltetrahydrofolate dehydrogenase, one of the major folate enzymes, is down-regulated in tumor tissues and possesses suppressor effects on cancer cells.". Cell Growth Differ. 13 (5): 227–36. PMID 12065246.
Hong M, Lee Y, Kim JW, et al. (1999). "Isolation and characterization of cDNA clone for human liver 10-formyltetrahydrofolate dehydrogenase.". Biochem. Mol. Biol. Int. 47 (3): 407–15. doi:10.1080/15216549900201433. PMID 10204077.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Champion KM, Cook RJ, Tollaksen SL, Giometti CS (1994). "Identification of a heritable deficiency of the folate-dependent enzyme 10-formyltetrahydrofolate dehydrogenase in mice". Proc. Natl. Acad. Sci. U.S.A. 91 (24): 11338–42. doi:10.1073/pnas.91.24.11338. PMC 45226. PMID 7972060.
Johlin FC, Swain E, Smith C, Tephly TR (1989). "Studies on the mechanism of methanol poisoning: purification and comparison of rat and human liver 10-formyltetrahydrofolate dehydrogenase". Mol. Pharmacol. 35 (6): 745–50. PMID 2733692.

PDB gallery

1s3i: Crystal structure of the N terminal hydrolase domain of 10-formyltetrahydrofolate dehydrogenase

2bw0: CRYSTAL STRUCTURE OF THE HYDROLASE DOMAIN OF HUMAN 10-FORMYLTETRAHYDROFOLATE 2 DEHYDROGENASE

2cfi: THE HYDROLASE DOMAIN OF HUMAN 10-FTHFD IN COMPLEX WITH 6-FORMYLTETRAHYDROPTERIN

2cq8: Solution structure of RSGI RUH-033, a pp-binding domain of 10-FTHFDH from human cDNA

2o2p: Crystal structure of the C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase

2o2q: Crystal structure of the C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADP

2o2r: Crystal structure of the C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH

Aldehyde dehydrogenases (EC 1.2.1)

Family 1	Retinaldehyde — ALDH1A1 ALDH1A2 ALDH1A3 ALDH1B1 Formyltetrahydrofolate — ALDH1L1 ALDH1L2

Family 2 (mitochondrial)	ALDH2

Family 3	Dimeric NADP-preferring — (ALDH3A1) Fatty aldehyde — (ALDH3A2) ALDH3B1 ALDH3B2

Other	ALDH4A1 ALDH5A1 ALDH6A1 α-Aminoadipic semialdehyde — (ALDH7A1) ALDH8A1 ALDH9A1 ALDH16A1 ALDH18A1 Glyceraldehyde 3-phosphate — (GAPDH)

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ALDH1L1

References

Further reading