| ID | Sequence | Length | GC content |
|---|---|---|---|
| CCCUGCUCGGCGCUGCCCGCCCAGUUCCUGUUCCCAGACUGAGGCCCAG… | 2150 nt | 0.5549 | |
| CUGGAGGGAGGGGCGUGGAUACAGCGGGAAAGGAGAGACCCCUAGCGGG… | 2368 nt | 0.5612 | |
| GCAAACUGGCGGCGUGCUCCGCGGGAGAGCACACCUGGCCACGGCCUGG… | 3270 nt | 0.5450 | |
| GCAAACUGGCGGCGUGCUCCGCGGGAGAGCACACCUGGCCACGGCCUGG… | 3092 nt | 0.5517 | |
| GCAAACUGGCGGCGUGCUCCGCGGGAGAGCACACCUGGCCACGGCCUGG… | 3281 nt | 0.5443 | |
| CCCUGCUCGGCGCUGCCCGCCCAGUUCCUGUUCCCAGACUGAGGCCCAG… | 1774 nt | 0.5586 |
S-adenosylhomocysteine hydrolase belongs to the adenosylhomocysteinase family. It catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) to adenosine (Ado) and L-homocysteine (Hcy). Thus, it regulates the intracellular S-adenosylhomocysteine (SAH) concentration thought to be important for transmethylation reactions. Deficiency in this protein is one of the different causes of hypermethioninemia. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jun 2009]
A study in mice demonstrated that in vivo α-particle irradiation of Kupffer or endothelial liver cells induced a characteristic inflammatory state and altered gene expression profiles, with the AHCY (S-adenosylhomocysteine hydrolase) being commonly down-regulated following Kupffer cell-specific and endothelial cell-specific exposures to α-particles [Roudkenar et al. DOI:10.1269/jrr.07078].