AASS

Aminoadipate-semialdehyde synthase
Identifiers
Symbols	AASS; LKR/SDH; LKRSDH; LORSDH
External IDs	OMIM: 605113 MGI: 1353573 HomoloGene: 4212 GeneCards: AASS Gene
Gene Ontology Molecular function • binding • oxidoreductase activity • saccharopine dehydrogenase (NADP+, L-lysine-forming) activity • saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity • saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity Cellular component • cytoplasm • mitochondrion • mitochondrion • mitochondrial matrix • intracellular membrane-bounded organelle Biological process • lysine catabolic process • lysine catabolic process • L-lysine catabolic process • cellular nitrogen compound metabolic process • protein tetramerization Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10157	30956
Ensembl	ENSG00000008311	ENSMUSG00000029695
UniProt	Q9UDR5	Q3UEQ9
RefSeq (mRNA)	NM_005763	NM_013930.4
RefSeq (protein)	NP_005754	NP_038958.2
Location (UCSC)	Chr 7: 121.72 – 121.78 Mb	Chr 6: 23.02 – 23.08 Mb
PubMed search	[1]	[2]

Alpha-aminoadipic semialdehyde synthase, mitochondrial is an enzyme that in humans is encoded by the AASS gene.

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.

Further reading

• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• Hillier LW, Fulton RS, Fulton LA, et al. (2003). "The DNA sequence of human chromosome 7". Nature 424 (6945): 157–64. doi:10.1038/nature01782. PMID 12853948. 
• Scherer SW, Cheung J, MacDonald JR, et al. (2003). "Human Chromosome 7: DNA Sequence and Biology". Science 300 (5620): 767–72. doi:10.1126/science.1083423. PMC 2882961. PMID 12690205. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2882961. 
• Papes F, Kemper EL, Cord-Neto G, et al. (2000). "Lysine degradation through the saccharopine pathway in mammals: involvement of both bifunctional and monofunctional lysine-degrading enzymes in mouse". Biochem. J. 344 Pt 2 (Pt 2): 555–63. PMC 1220675. PMID 10567240. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1220675. 
• "Toward a complete human genome sequence". Genome Res. 8 (11): 1097–108. 1999. doi:10.1101/gr.8.11.1097. PMID 9847074. 
• 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. doi:10.1016/S0378-1119(97)00411-3. 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. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.