Overview of structurally homologous flavoprotein oxidoreductases containing the low Mr thioredoxin reductase-like fold – A functionally diverse group

Structural studies show that enzymes have a limited number of unique folds, although structurally related evolved to perform large variety functions. In this review, we focused on containing the low molecular weight thioredoxin reductase (low Mr TrxR) fold. This fold consists two domains, both three-layer ??? sandwich Rossmann-like fold, serving as flavin adenine dinucleotide (FAD) and, in most cases, pyridine nucleotide (NAD(P)H) binding-domains. Based search Protein Data Bank for all published structures TrxR-like here present comprehensive overview with structural architecture. These range from ferredoxin/flavodoxin NAD(P)+ oxidoreductases, through glutathione reductase, NADH peroxidase. Some are solely composed while others contain one or additional domains. give detailed description selected only however, catalyzing diversity chemical reactions. Our similar, yet functionally distinct group flavoprotein oxidoreductases highlights fascinating and increasing describing among these enzymes, especially during last decade(s).