ALDH1L1

From Wikipedia, the free encyclopedia

Aldehyde dehydrogenase 1 family, member L1

PDB rendering based on 1s3i.

Available structures: 1s3i, 2bw0, 2cfi, 2cq8, 2o2p, 2o2q, 2o2r

Identifiers

Symbol(s)

ALDH1L1; DKFZp781N0997; FTHFD

External IDs

OMIM: 600249 MGI: 1340024 HomoloGene: 56553

Gene ontology
Molecular Function:	• methyltransferase activity • formyltetrahydrofolate dehydrogenase activity • oxidoreductase activity • hydroxymethyl-, formyl- and related transferase activity • cofactor binding
Cellular Component:	• cytoplasm
Biological Process:	• translation • one-carbon compound metabolic process • biosynthetic process • 10-formyltetrahydrofolate catabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_012190 (mRNA)
NP_036322 (protein)

XM_994115 (mRNA)
XP_999209 (protein)

Location

Chr 3: 127.31 - 127.38 Mb

Chr 6: 90.52 - 90.56 Mb

Pubmed search

[1]

[2]

Aldehyde dehydrogenase 1 family, member L1, also known as ALDH1L1, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: ALDH1L1 aldehyde dehydrogenase 1 family, member L1.

[edit] Further reading

Lee KM, Lan Q, Kricker A, et al.. "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. 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. 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. 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. 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. 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. 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.