ALDH1L1

10-formyltetrahydrofolate dehydrogenase is an enzyme that in humans is encoded by the ALDH1L1 gene.[5]

ALDH1L1
Available structures PDB 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	OMIM: 600249 MGI: 1340024 HomoloGene: 122031 GeneCards: ALDH1L1
Gene location (Human) Chr. Chromosome 3 (human)[1] Band 3q21.3 Start 126,103,562 bp[1] End 126,197,994 bp[1]
Gene location (Mouse) Chr. Chromosome 6 (mouse)[2] Band 6|6 D1 Start 90,486,427 bp[2] End 90,600,203 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • formyltetrahydrofolate dehydrogenase activity • oxidoreductase activity • hydroxymethyl-, formyl- and related transferase activity • catalytic activity • aldehyde dehydrogenase (NAD) activity • oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor Cellular component • extracellular exosome • mitochondrion • cytoplasm • cytosol Biological process • metabolism • one-carbon metabolic process • biosynthetic process • 10-formyltetrahydrofolate catabolic process • oxidation-reduction process • folic acid metabolic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10840	107747
Ensembl	ENSG00000144908	ENSMUSG00000030088
UniProt	O75891	Q8R0Y6
RefSeq (mRNA)	NM_001270364 NM_001270365 NM_012190	NM_027406 NM_001356412
RefSeq (protein)	NP_001257293 NP_001257294 NP_036322	NP_081682 NP_001343341
Location (UCSC)	Chr 3: 126.1 – 126.2 Mb	Chr 6: 90.49 – 90.6 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[5]

References

1. GRCh38: Ensembl release 89: ENSG00000144908 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000030088 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: ALDH1L1 aldehyde dehydrogenase 1 family, member L1".

External links

• Human ALDH1L1 genome location and ALDH1L1 gene details page in the UCSC Genome Browser.

Further reading

• 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.