Functional and Phylogenetic Divergence of Fungal Adenylate-Forming Reductases

• DOI: 10.1128/aem.01767-14
• Publication Date: 2014-08-02T08:23:47Z
• Authors: Daniel Kalb; Gerald Lackner; Dirk Hoffmeister
• Keywords: Adenylylation; Aspergillus nidulans

A key step in fungal L-lysine biosynthesis is catalyzed by adenylate-forming L-α-aminoadipic acid reductases, organized domains for adenylation, thiolation, and the reduction step. However, genomes of numerous ascomycetes basidiomycetes contain an unexpectedly large number additional genes encoding similar but functionally distinct enzymes. Here, we describe functional vitro characterization four reductases which were heterologously produced Escherichia coli. The Ceriporiopsis subvermispora serine reductase Nps1 features a terminal ferredoxin-NADP+ (FNR) domain thus belongs to hitherto undescribed class multidomain second major characterized canonical short-chain dehydrogenase/reductase represented Nps3 as first biochemically basidiomycete origin. Aspergillus flavus l-tyrosine LnaA LnbA are members phylogenetic clade. Phylogenetic analysis supports view that more diverse than previously recognized belong classes.