| Standard Name | LYS12 1 |
|---|---|
| Systematic Name | YIL094C |
| Alias | LYS10 , LYS11 |
| Feature Type | ORF, Verified |
| Description | Homo-isocitrate dehydrogenase, an NAD-linked mitochondrial enzyme required for the fourth step in the biosynthesis of lysine, in which homo-isocitrate is oxidatively decarboxylated to alpha-ketoadipate (2 and see Summary Paragraph) |
| Name Description | LYSine requiring 1 |
| Chromosomal Location | |
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| Note: this feature is encoded on the Crick strand. | |
| View Computational GO annotations for LYS12 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| High-throughput |
| Pathways |
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| Classical genetics | |
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| null |
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| Large-scale survey | |
| null |
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| Resources |
| 74 total interaction(s) for 68 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| Resources |
| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
| Note: this feature is encoded on the Crick strand. | |||||||||||||
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| Last Update | Coordinates: 2011-02-03 | Sequence: 1994-12-10 | ||||||||||||
| Subfeature details |
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| S288C only | |
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| S288C vs. other species | |
| S288C vs. other strains |
| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000001356 |
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About lysine biosynthesis
S. cerevisiae synthesizes the essential amino acid L-lysine via the L-alpha-aminoadipic acid pathway instead of the diaminopmelate pathway (3). Originally proposed to be characteristic of fungi, recent studies suggest prokaryotes also synthesize lysine via the alpha-aminoadipic acid pathway (4). Intermediates in this pathway are often incorporated into secondary metabolites. For example, it has been well- studied that alpha-aminoadipate is required for penicillin production (3). Regulation of the lysine biosynthetic pathway in S. cerevisiae is an interaction between general amino acid control (via Gcn4p) (5), feedback inhibition of homocitrate synthase activity by lysine (6), and induction of Lys14p by alpha-aminoadipate semialdehyde (7).
| 1) | Jonkers, H., et al. (1998) Identification of YIL094C as the gene for homo-isocitrate dehydrogenase (LYS12) in Saccharomyces cerevisiae |
| 2) | Strassman M and Ceci LN (1965) Enzymatic formation of alpha-ketoadipic acid from homoisocitric acid. J Biol Chem 240(11):4357-61 |
| 3) | Zabriskie TM and Jackson MD (2000) Lysine biosynthesis and metabolism in fungi. Nat Prod Rep 17(1):85-97 |
| 4) | Nishida H and Nishiyama M (2000) What is characteristic of fungal lysine synthesis through the alpha-aminoadipate pathway? J Mol Evol 51(3):299-302 |
| 5) | Hinnebusch A (1992) "General and Pathway-specific Regulatory Mechanisms Controlling the Synthesis of Amino Acid Biosynthetic Enzymes in Saccharomyces cerevisiae". Pp. 319-414 in The Molecular and Cellular Biology of the Yeast Saccharomyces: Gene Expression, edited by Jones EW, Pringle JR and Broach JR. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press |
| 6) | Feller A, et al. (1999) In Saccharomyces cerevisae, feedback inhibition of homocitrate synthase isoenzymes by lysine modulates the activation of LYS gene expression by Lys14p. Eur J Biochem 261(1):163-70 |
| 7) | El Alami M, et al. (2000) Characterisation of a tripartite nuclear localisation sequence in the regulatory protein Lys14 of Saccharomyces cerevisiae. Curr Genet 38(2):78-86 |





