ArticleApplied and environmental microbiology2014
Functional and phylogenetic divergence of fungal adenylate-forming reductases.
Article in Applied and environmental microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 37 citations in OpenAlex.
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- Bacillus sp.: A Remarkable Source of Bioactive Lipopeptides.Advances in biochemical engineering/biotechnology · 2022Article
- Molecular Evolution of Lysine Biosynthesis in Agaricomycetes.Journal of fungi (Basel, Switzerland) · 2021Article
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- Bacterial-Like Nonribosomal Peptide Synthetases Produce Cyclopeptides in the Zygomycetous Fungus Mortierella alpina.Applied and environmental microbiology · 2021Article
- Discovery and biosynthesis of guanipiperazine from a NRPS-like pathway.Chemical science · 2021Article
- Identification of a conserved N-terminal domain in the first module of ACV synthetases.MicrobiologyOpen · 2021Article
- Recent advances in biocatalytic derivatization of L-tyrosine.Applied microbiology and biotechnology · 2020Review
- Genome description of Phlebia radiata 79 with comparative genomics analysis on lignocellulose decomposition machinery of phlebioid fungi.BMC genomics · 2019Article
- Structural basis of the nonribosomal codes for nonproteinogenic amino acid selective adenylation enzymes in the biosynthesis of natural products.Journal of industrial microbiology & biotechnology · 2019Review
- Plant-like biosynthesis of isoquinoline alkaloids in Aspergillus fumigatus.Nature chemical biology · 2016Article
- Biocatalytic portfolio of Basidiomycota.Current opinion in chemical biology · 2016Review
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3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A key step in fungal L-lysine biosynthesis is catalyzed by adenylate-forming L-α-aminoadipic acid reductases, organized in domains for adenylation, thiolation, and the reduction step. However, the genomes of numerous ascomycetes and basidiomycetes contain an unexpectedly large number of additional genes encoding similar but functionally distinct enzymes. Here, we describe the functional in vitro characterization of four reductases which were heterologously produced in Escherichia coli. The Ceriporiopsis subvermispora serine reductase Nps1 features a terminal ferredoxin-NADP+ reductase (FNR) domain and thus belongs to a hitherto undescribed class of fungal multidomain enzymes. The second major class is characterized by the canonical terminal short-chain dehydrogenase/reductase domain and represented by Ceriporiopsis subvermispora Nps3 as the first biochemically characterized L-α-aminoadipic acid reductase of basidiomycete origin. Aspergillus flavus l-tyrosine reductases LnaA and LnbA are members of a distinct phylogenetic clade. Phylogenetic analysis supports the view that fungal adenylate-forming reductases are more diverse than previously recognized and belong to four distinct classes.
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