What Is Characteristic of Fungal Lysine Synthesis Through the α-Aminoadipate Pathway?

  title={What Is Characteristic of Fungal Lysine Synthesis Through the $\alpha$-Aminoadipate Pathway?},
  author={Hiromi Nishida and Makoto Nishiyama},
  journal={Journal of Molecular Evolution},
Abstract. Recent finding that a prokaryote synthesizes lysine through the α-aminoadipate pathway demonstrates that the lysine synthesis through the α-aminoadipate pathway is not typical of fungi. However, the fungal lysine biosynthesis is not completely the same as the prokaryotic one. We point out that α-aminoadipate reductase is a key enzyme to the evolution of fungal lysine synthesis. In addition, fungi have two different saccharopine dehydrogenases, which is also characteristic of fungi. 
The α-aminoadipate pathway for lysine biosynthesis in fungi
The α-aminoadipate pathway is unique to fungi and is thus a potential target for the rational design of antifungal drugs.
LysY : the best marker of prokaryotic lysine biosynthesis through the aminoadipate pathway
It is revealed that LysY is a key enzyme to the evolution of prokaryotic lysine biosynthesis through the aminoadipate pathway, and is the most useful marker of this pathway.
Specialization of the paralogue LYS21 determines lysine biosynthesis under respiratory metabolism in Saccharomyces cerevisiae.
It can be concluded that retention and further biochemical specialization of the LYS20- and LYS21-encoded enzymes with partially overlapping roles contributed to the acquisition of facultative metabolism.
Molecular Evolution of Lysine Biosynthesis in Agaricomycetes
The evolution of the α-aminoadipic acid pathway of lysine biosynthesis is consistent with the evolution of species at the order level in Agaricomycetes, and the conservation of primary, secondary, predicted tertiary structures, and substrate-binding sites of the enzymes of HCS, AAR, and SDH exhibited the evolutionary conservation of lynium biosynthesis.
Comparative Analyses of Homocitrate Synthase Genes of Ascomycetous Yeasts
  • H. Nishida
  • Biology
    International journal of evolutionary biology
  • 2012
Phylogenetic analysis showed that duplication has occurred multiple times during evolution of the ascomycetous yeasts and it is likely that HCS gene duplication in S. cerevisiae has maintained HCS activity for lysine biosynthesis and has obtained bifunctionality.
Structural characterization and comparison of three acyl-carrier-protein synthases from pathogenic bacteria
An interesting finding is a crystal artifact related to the activity of the enzyme that fortuitously represents an opportunity for a strategy to design a potential inhibitor of a pathogenic AcpS.
Molecular evolution of adenylating domain of aminoadipate reductase
The lys2 gene is one of the most useful tools for revealing the phylogenetic relationships among fungi, due to its low insertion/deletion rate and its high substitution rate.
Aminoadipate reductase gene: a new fungal-specific gene for comparative evolutionary analyses
This study designed degenerate primers for polymerase chain reaction (PCR) amplification of a large fragment of the aminoadipate reductase gene for divergent fungi and constructed phylogenetic trees that are consistent with current ascomycete systematics.
Different elongation pathways in the biosynthesis of acyl groups of trichome exudate sugar esters from various solanaceous plants
Results are consistent with participation of αKAE in synthesis of sugar-ester acyl groups of tobaccos and petunia, but apparently FAS is utilized in the formation of these groups in L. pennellii and D. metel.


[157] Lysine biosynthesis (yeast)
Lysine is synthesized through the α-aminoadipate pathway in Thermus thermophilus
Results indicate that lysine was synthesized through the α-aminoadipate pathway and not through the diaminopimelate pathway in T. thermophilus, which was disrupted by integration of the heat-stable kanamycin nucleotidyltransferase gene.
The LYS5 gene of Saccharomyces cerevisiae.
Lysine degradation through the saccharopine pathway in mammals: involvement of both bifunctional and monofunctional lysine-degrading enzymes in mouse.
Sequence analyses show that the bifunctional enzyme is likely to be a mitochondrial protein, and enzymic and expression analyses suggest that lysine-oxoglutarate reductase/saccharopine dehydrogenase levels increase in livers of mice under starvation.
Molecular analysis of the LYS2 gene of Candida albicans: homology to peptide antibiotic synthetases and the regulation of the ⋅-aminoadipate reductase
The LYS2 mRNA and α-aminoadipate reductase activity were repressed to a higher level in YEPD-grown cells than in cells grown in the presence of lysine or minimal medium, and AAR was shown to be feedback-inhibited by lYSine and the lysinesine analog, thialysine.
A prokaryotic gene cluster involved in synthesis of lysine through the amino adipate pathway: a key to the evolution of amino acid biosynthesis.
This gene cluster was analogous in part to the present leucine and arginine biosyntheses pathways and is assumed to be one of the origins of lysine biosynthesis and could therefore become a key to the evolution of amino acid biosynthesis.
Lysine Biosynthesis and Evolution
Distribution of Lysine Pathways Among Fungi: Evolutionary Implications
  • H. Vogel
  • Biology
    The American Naturalist
  • 1964
The remarkable consistency of the distribution of the two lysine paths suggests that (a) they did not arise sporadically; (b) their distribution pattern was not disturbed by genetic exchange; and (c) there is a substantial evolutionary gap in organisms differing in path of l Lysine synthesis.
Aspartate Kinase-Independent Lysine Synthesis in an Extremely Thermophilic Bacterium, Thermus thermophilus: Lysine Is Synthesized via α-Aminoadipic Acid Not via Diaminopimelic Acid
Results indicated that in T. thermophilus, lysine was not synthesized via the diaminopimelic acid pathway, believed to be common to all bacteria, but via a pathway using alpha-aminoadipic acid as a biosynthetic intermediate.