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Chemical Compound Review:

L-allysine (2S)-2-amino-6-oxo-hexanoic acid

Synonyms: AG-K-70461, CHEBI:17917, AC1Q6QJV, AC-12923, CTK0H6818, ...

Sacksteder, K.A. et al., Suvarna, K. et al., Kinzel, J.J. et al., Akagawa, M. et al., Kinzel, J.J. et al., et al.

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Disease relevance of alpha-Aminoadipic semialdehyde

Identification of the alpha-aminoadipic semialdehyde synthase gene, which is defective in familial hyperlysinemia [1].
Such oxidative modifications are a major contributing factor to diabetic complications and aging. alpha-Aminoadipic semialdehyde (AAS) and gamma-glutamic semialdehyde (GGS) have been identified as the major carbonyl products in oxidized proteins both in vitro and in vivo [2].

High impact information on alpha-Aminoadipic semialdehyde

This bifunctional protein has previously been referred to as "alpha-aminoadipic semialdehyde synthase," and we have tentatively designated this gene "AASS." The AASS cDNA contains an open reading frame of 2,781 bp predicted to encode a 927-amino-acid-long protein [1].
Lysyl oxidase initiates the covalent cross-linking of elastin and collagen by oxidizing lysine residues in these proteins to alpha-aminoadipic-delta-semialdehyde [3].
Lysyl oxidase catalyzes the oxidation of peptidyl lysine to alpha-aminoadipic-delta-semialdehyde, the precursor to the covalent crosslinkages that stabilize fibers of elastin and collagen [4].
Wild-type and saccharopine dehydrogenaseless mutant strains of Rhodotorula glutinis grew in minimal medium containing lysine as the sole nitrogen source and simultaneously accumulated, in the culture supernatant, large amounts of a product identified as alpha-aminoadipic-delta-semialdehyde [5].
Pipecolic acid oxidase from Rhodotorula glutinis, which converts pipecolic acid to alpha-aminoadipic-delta-semialdehyde, an intermediate of the biosynthetic pathway of lysine, was purified 290-fold [6].

Associations of alpha-Aminoadipic semialdehyde with other chemical compounds

The unique alpha-aminoadipate pathway for lysine biosynthesis is present only in fungi and involves eight enzyme steps. alpha-Aminoadipate semialdehyde dehydrogenase, commonly called alpha-aminoadipate reductase (AAR), catalyzes the conversion of alpha-aminoadipic acid to alpha-aminoadipic semialdehyde by a novel mechanism [7].

References

Identification of the alpha-aminoadipic semialdehyde synthase gene, which is defective in familial hyperlysinemia. Sacksteder, K.A., Biery, B.J., Morrell, J.C., Goodman, B.K., Geisbrecht, B.V., Cox, R.P., Gould, S.J., Geraghty, M.T. Am. J. Hum. Genet. (2000) [Pubmed]
Formation of alpha-aminoadipic and gamma-glutamic semialdehydes in proteins by the maillard reaction. Akagawa, M., Sasaki, D., Kurota, Y., Suyama, K. Ann. N. Y. Acad. Sci. (2005) [Pubmed]
Influence of sequence and charge on the specificity of lysyl oxidase toward protein and synthetic peptide substrates. Kagan, H.M., Williams, M.A., Williamson, P.R., Anderson, J.M. J. Biol. Chem. (1984) [Pubmed]
Properties and function of lysyl oxidase. Kagan, H.M., Trackman, P.C. Am. J. Respir. Cell Mol. Biol. (1991) [Pubmed]
Role of L-lysine-alpha-ketoglutarate aminotransferase in catabolism of lysine as a nitrogen source for Rhodotorula glutinis. Kinzel, J.J., Winston, M.K., Bhattacharjee, J.K. J. Bacteriol. (1983) [Pubmed]
Lysine biosynthesis in Rhodotorula glutinis: properties of pipecolic acid oxidase. Kinzel, J.J., Bhattacharjee, J.K. J. Bacteriol. (1982) [Pubmed]
Molecular analysis of the LYS2 gene of Candida albicans: homology to peptide antibiotic synthetases and the regulation of the alpha-aminoadipate reductase. Suvarna, K., Seah, L., Bhattacherjee, V., Bhattacharjee, J.K. Curr. Genet. (1998) [Pubmed]

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