Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/85102
標題: The phylogenetic analysis and putative function of lysine 2,3-aminomutase from methanoarchaea infers the potential biocatalysts for the synthesis of β-lysine
關鍵字: Archaea
β-lysine
Biocatalysts
Lysine 2,3-aminomutase
Methanogen
摘要: Background: b-amino acids play important biological roles as precursors in the biosynthesis ofantibiotics, anticancer agents, neurotransmitters, and other high molecular weight polymers.Microbial cells and enzymes from extreme environments offer new opportunities forbiocatalysis and biotransformations as a result of their extreme stability. Lysine 2,3-aminomutase catalyzes the interconversion of L-a-lysine and L-b-lysine. L-b-lysine isa precursor in the bacterial biosynthesis of several antibiotics, and also is a precursor in thebiosynthesis of osmolyte Nε-acetyl-b-lysine for salt stress and adaptation in methanoarchaea.Methods: Lysine 2,3-aminomutase (AblA) genes from the marine Methanosarcina mazeiN2M9705, halotolerant Methanocalculus chunghsingensis K1F9705bT, and halophilic Methanohalophilusportucalensis FDF1T were cloned by PCR and southern hybridization. Both nucleotideand amino acid sequences of AblAs were analyzed and phylogenetic comparisonsperformed. Additionally, the functional motifs and 3D structure of aminomutases were alignedand compared.Results: The deduced amino acid sequences of AblAs from methanoarchaea share high identitywith the known clostridial and Bacillus lysine 2,3-aminomutase. The conserved amino acidresidues for cofactors, such as the iron-sulfur cluster, S-adenosylmethionine (SAM), pyridoxal5’-phosphate (PLP) and zinc-binding sites in methanoarchaeal AblAs suggested that they werelysine 2,3-aminomutases.Conclusion: AblAs from methanoarchaea are lysine 2,3-aminomutases that may function aspotential biocatalysts for the synthesis of b-lysine in vivo and in vitro.
URI: http://hdl.handle.net/11455/85102
文章連結: http://dx.doi.org/10.1016/j.jmii.2011.12.031
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