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(Top)
 


1 Pathway overview  





2 See also  





3 References  














α-Aminoadipate pathway






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From Wikipedia, the free encyclopedia
 

(Redirected from Α-aminoadipate pathway)

The amino acid L-lysine

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 several species of yeast, higher fungi (containing chitin in their cell walls), and the euglenids.[1][2][3][4][5] It has also been reported from bacteria of the genus Thermus[6] and also in Pyrococcus horikoshii,[7] potentially suggesting a wider distribution than previously thought. This uniqueness of the pathway makes it a potentially interesting target for antimycotics.[3]

Pathway overview[edit]

Comparison of parts of the diaminopimelate (DAP) pathway (left) and α-aminoadipate (AAA) pathway (right).

This pathway is a part of the glutamate family of amino acid biosynthetic pathways.[2] The reaction steps in the pathway are similar to the citric acid cycle.

The first step in the pathway is condensation of acetyl-CoA with α-ketoglutarate, which gives homocitrate. This reaction is catalyzed by homocitrate synthase. Homocitrate is then converted to homoaconitatebyhomoaconitase and then to homoisocitrate. This is then decarboxylatedbyhomoisocitrate dehydrogenase, which results in α-ketoadipate. A nitrogen atom is added from glutamate by aminoadipate aminotransferase to form the α-aminoadipate, 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.[2]

Conversion of lysine to α-ketoadipate during degradation of lysine proceeds via the same steps, but in reverse.[8]

See also[edit]

References[edit]

  1. ^ Zabriskie TM, Jackson MD (2000). "Lysine biosynthesis and metabolism in fungi". Natural Product Reports. 17 (1): 85–97. doi:10.1039/a801345d. PMID 10714900.
  • ^ a b c Xu H, Andi B, Qian J, West AH, Cook PF (2006). "The alpha-aminoadipate pathway for lysine biosynthesis in fungi". Cell Biochemistry and Biophysics. 46 (1): 43–64. doi:10.1385/CBB:46:1:43. PMID 16943623. S2CID 22370361.
  • ^ a b Andi B, West AH, Cook PF (September 2004). "Kinetic mechanism of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae". Biochemistry. 43 (37): 11790–11795. doi:10.1021/bi048766p. PMID 15362863.
  • ^ Bhattacharjee JK (1985). "alpha-Aminoadipate pathway for the biosynthesis of lysine in lower eukaryotes". Critical Reviews in Microbiology. 12 (2): 131–151. doi:10.3109/10408418509104427. PMID 3928261.
  • ^ Bhattacharjee JK, Strassman M (May 1967). "Accumulation of tricarboxylic acids related to lysine biosynthesis in a yeast mutant". The Journal of Biological Chemistry. 242 (10): 2542–2546. doi:10.1016/S0021-9258(18)95997-1. PMID 6026248.
  • ^ 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.
  • ^ Nishida, Hiromi; Nishiyama, Makoto; Kobashi, Nobuyuki; Kosuge, Takehide; Hoshino, Takayuki; Yamane, Hisakazu (1999-12-01). "A Prokaryotic Gene Cluster Involved in Synthesis of Lysine through the Amino Adipate Pathway: A Key to the Evolution of Amino Acid Biosynthesis". Genome Research. 9 (12): 1175–1183. doi:10.1101/gr.9.12.1175. ISSN 1088-9051. PMID 10613839.
  • ^ Voet, Donald; Voet, Judith G. (2011). Biochemistry (4. ed.). Hoboken, NJ: Wiley. ISBN 978-0-470-91745-9.
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