Evidence for gene duplication forming similar binding folds for NAD(P)H and FAD in pyridine nucleotide-dependent flavoenzymes.
For pyridine nucleotide-dependent flavoenzymes, binding both FAD and NAD(P)H on a single amino-acid chain, we have found a high degree of internal sequence similarity for certain regions of the FAD and NAD(P)H binding portions of the chain for any given protein. This was the case for a range of enzyme classes, including disulphide oxidoreductases (such as glutathione reductase, trypanothione reductase, lipoamide dehydrogenase, mercuric reductase), mono- and dioxygenases, nitrite reductase, alkyl hydroperoxidase and NADH dehydrogenase from E. coli. This provides strong support for gene duplication as the origin of at least part of the FAD and NAD(P)H recognising domains of such enzymes.
McKie
J H
JH
Department of Pharmacy, University of Manchester, UK.
Douglas
K T
KT
D000595:Amino Acid Sequence; D000818:Animals; D001419:Bacteria / Q000201:enzymology; D001665:Binding Sites; D004926:Escherichia coli / Q000201:enzymology; D005182:Flavin-Adenine Dinucleotide / Q000235:genetics*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D005810:Multigene Family; D009249:NADP / Q000235:genetics*; D010088:Oxidoreductases / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid; D013552:Swine
D005182:Flavin-Adenine Dinucleotide; D009249:NADP; D010088:Oxidoreductases