||It has been suggested that Homoisocitrate be merged into this article. (Discuss) Proposed since April 2013.|
The α-aminoadipate pathway is a biochemical pathway for the synthesis of the amino acid L-lysine. In the eukaryotes, this pathway is unique to the higher fungi (containing chitin in their cell walls) and the euglenids. It has also been reported from bacteria of the genus Thermus.
Homocitrate is initially synthesised from acetyl-CoA and 2-oxoglutarate by homocitrate synthase. This is then converted to homoaconitate by homoaconitase and then to homoisocitrate by homoisocitrate dehydrogenase. A nitrogen atom is added from glutamate by aminoadipate aminotransferase to form the α-amnoadipate from which this pathway gets its name. This is then reduced by aminoadipate reductase via an acyl-enzyme intermediate to a semialdehyde. Reaction with glutamate by one class of saccharopine dehydrogenase yields saccharopine which is then cleaved by a second saccharopine dehydrogenase to yield lysine and oxoglutarate.
- Zabriskie TM, Jackson MD. (2000). "Lysine biosynthesis and metabolism in fungi". Natural Product Reports 17 (1): 85–97. doi:10.1039/a801345d. PMID 10714900.
- Kosuge T, Hoshino T (1999). "The α-aminoadipate pathway for lysine biosynthesis is widely distributed among Thermus strains". Journal of Bioscience and Bioengineering 88 (6): 672–5. doi:10.1016/S1389-1723(00)87099-1. PMID 16232683.
- Xu H, Andi B, Qian J, West AH, Cook PF (2006). "The α-aminoadipate pathway for lysine biosynthesis in fungi". Cell Biochemistry and Biophysics 46 (1): 43–64. doi:10.1385/CBB:46:1:43. PMID 16943623.
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