SAM1 BASIC INFORMATION
| Standard Name | SAM1 1 |
|---|---|
| Systematic Name | YLR180W |
| Alias | ETH10 |
| Feature Type | ORF, Verified |
| Description | S-adenosylmethionine synthetase, catalyzes transfer of the adenosyl group of ATP to the sulfur atom of methionine; one of two differentially regulated isozymes (Sam1p and Sam2p) (2, 3, 4 and see Summary Paragraph)
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| Name Description | S-AdenosylMethionine requiring 5 |
| GO Annotations | All SAM1 GO evidence and references |
|---|---|
| View Computational GO annotations for SAM1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| High-throughput |
| Pathways |
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| Mutant Phenotype | All SAM1 Phenotype details and references |
|---|---|
| Classical genetics | |
| null | |
| Large-scale survey | |
| null |
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| Interactions | SAM1 All interactions details and references |
|---|---|
| 113 total interaction(s) for 76 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB |
|---|
| Primary SGDID | S000004170 |
|---|
ADDITIONAL INFORMATION for SAM1
SUMMARY PARAGRAPH for SAM1
SAM1 and SAM2 encode S-adenosylmethionine (AdoMet) synthetases (also known as methionine adenosyl transferases (MAT)), which catalyze the biosynthesis of AdoMet from methionine and ATP (5). AdoMet is involved in the methylation of proteins, RNAs, and lipids (6) as well as in the biosynthesis of biotin (7) and polyamines (8, 9). AdoMet is believed to participate in more reactions than any other cofactor with the exception of ATP (6).
Mutations in SAM1 or SAM2 do not affect growth; however, a sam1 sam2 double mutant results in AdoMet auxotrophy (5). Although SAM1 and SAM2 encode functionally equlvalent AdoMet synthetases, they are regulated differently (2). Both SAM1 and SAM2 are repressed by excess AdoMet, but expression of SAM2 increases during growth, which overrides the AdoMet-mediated repression (2). In addition, SAM2 is repressed by the addition of myo-inositol and choline, similar to a number of genes encoding enzymes involved in phospholipid biosynthesis (4). In contrast, SAM1 is not subject to the inositol-choline regulation suggesting that SAM2, but not SAM1, may be involved in phospholipid biosynthesis (4).
AdoMet synthetase is well conserved through evolution (from 2). In humans, deficiency in AdoMet synthetase results in the metabolic disease,
REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for SAM1]
| 1) | Rosenberg, N. and Rothstein, R. (1992) Personal Communication, Mortimer Map Edition 11 |
| 2) | Thomas D and Surdin-Kerjan Y (1991) The synthesis of the two S-adenosyl-methionine synthetases is differently regulated in Saccharomyces cerevisiae. Mol Gen Genet 226(1-2):224-32 |
| 3) | Thomas D and Surdin-Kerjan Y (1987) SAM1, the structural gene for one of the S-adenosylmethionine synthetases in Saccharomyces cerevisiae. Sequence and expression. J Biol Chem 262(34):16704-9 |
| 4) | Kodaki T, et al. (2003) Differential transcriptional regulation of two distinct S-adenosylmethionine synthetase genes (SAM1 and SAM2) of Saccharomyces cerevisiae. Nucleic Acids Res Suppl(3):303-4 |
| 5) | Cherest H and Surdin-Kerjan Y (1978) S-adenosyl methionine requiring mutants in Saccharomyces cerevisiae: evidences for the existence of two methionine adenosyl transferases. Mol Gen Genet 163(2):153-67 |
| 6) | Thomas D and Surdin-Kerjan Y (1997) Metabolism of sulfur amino acids in Saccharomyces cerevisiae. Microbiol Mol Biol Rev 61(4):503-32 |
| 7) | Phalip V, et al. (1999) Characterization of the biotin biosynthesis pathway in Saccharomyces cerevisiae and evidence for a cluster containing BIO5, a novel gene involved in vitamer uptake. Gene 232(1):43-51 |
| 8) | Chattopadhyay MK, et al. (2006) Methylthioadenosine and polyamine biosynthesis in a Saccharomyces cerevisiae meu1delta mutant. Biochem Biophys Res Commun 343(1):203-7 |
| 9) | Subhi AL, et al. (2003) Methylthioadenosine phosphorylase regulates ornithine decarboxylase by production of downstream metabolites. J Biol Chem 278(50):49868-73 |
| 10) | Foury F (1997) Human genetic diseases: a cross-talk between man and yeast. Gene 195(1):1-10 |




