ALDH1L1

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) Band 3q21.3 Start 126,103,562 bp End 126,197,994 bp
Gene location (Mouse) Chr. Chromosome 6 (mouse) Band 6|6 D1 Start 90,463,409 bp End 90,577,185 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of liver kidney parotid gland gastrocnemius muscle optic nerve gastric mucosa caudate nucleus amygdala body of pancreas putamen Top expressed in left lobe of liver kidney proximal tubule left colon intestinal villus jejunum adrenal gland white adipose tissue optic nerve subcutaneous adipose tissue More reference expression data BioGPS 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 biosynthesis 10-formyltetrahydrofolate catabolic 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_144776 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: 90.46 – 90.58 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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

The protein encoded by this gene catalyzes the conversion of 10-formyltetrahydrofolate, nicotinamide adenine dinucleotide phosphate (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.

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. S2CID 21487646.
• 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. S2CID 25945965.
• 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. Bibcode:2002PNAS...9916899M. 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. S2CID 10950424.
• 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. Bibcode:1994PNAS...9111338C. 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.