Aminoadipate-semialdehyde synthase, also known as AASS, is a human gene.cite web | title = Entrez Gene: AASS aminoadipate-semialdehyde synthase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10157| accessdate = ]

section_title =
summary_text = This gene encodes a bifunctional enzyme that catalyzes the first two steps in the mammalian lysine degradation pathway. The N-terminal and the C-terminal portions of this enzyme contain lysine-ketoglutarate reductase and saccharopine dehydrogenase activity, respectively, resulting in the conversion of lysine to alpha-aminoadipic semialdehyde. Mutations in this gene are associated with familial hyperlysinemia.cite web | title = Entrez Gene: AASS aminoadipate-semialdehyde synthase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10157| accessdate = ]


Further reading

citations =
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Hillier LW, Fulton RS, Fulton LA, "et al." |title=The DNA sequence of human chromosome 7. |journal=Nature |volume=424 |issue= 6945 |pages= 157–64 |year= 2003 |pmid= 12853948 |doi= 10.1038/nature01782
*cite journal | author=Scherer SW, Cheung J, MacDonald JR, "et al." |title=Human chromosome 7: DNA sequence and biology. |journal=Science |volume=300 |issue= 5620 |pages= 767–72 |year= 2003 |pmid= 12690205 |doi= 10.1126/science.1083423
*cite journal | author=Sacksteder KA, Biery BJ, Morrell JC, "et al." |title=Identification of the alpha-aminoadipic semialdehyde synthase gene, which is defective in familial hyperlysinemia. |journal=Am. J. Hum. Genet. |volume=66 |issue= 6 |pages= 1736–43 |year= 2001 |pmid= 10775527 |doi=
*cite journal | author=Papes F, Kemper EL, Cord-Neto G, "et al." |title=Lysine degradation through the saccharopine pathway in mammals: involvement of both bifunctional and monofunctional lysine-degrading enzymes in mouse. |journal=Biochem. J. |volume=344 Pt 2 |issue= |pages= 555–63 |year= 2000 |pmid= 10567240 |doi=
*cite journal | author= |title=Toward a complete human genome sequence. |journal=Genome Res. |volume=8 |issue= 11 |pages= 1097–108 |year= 1999 |pmid= 9847074 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=

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