Protein engineering of domains in flavoprotein disulphide oxidoreductases: contributions to folding and assembly.
Perham
R N
RN
Cambridge Centre for Molecular Recognition, Department of Biochemistry, University of Cambridge, U.K.
Leistler
B
B
Solomon
R G
RG
Guptasarma
P
P
D000123:Acetyltransferases / Q000737:chemistry; D016948:Azotobacter vinelandii / Q000201:enzymology; D008058:Dihydrolipoamide Dehydrogenase / Q000737:chemistry; D051047:Dihydrolipoyllysine-Residue Acetyltransferase; D004220:Disulfides / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology; D005420:Flavoproteins / Q000096:biosynthesis / Q000737:chemistry*; D001411:Geobacillus stearothermophilus / Q000201:enzymology; D005980:Glutathione Reductase / Q000737:chemistry; D008961:Models, Structural; D009247:NADH, NADPH Oxidoreductases / Q000096:biosynthesis / Q000737:chemistry*; D017354:Point Mutation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011768:Pyruvate Dehydrogenase Complex; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry*
D004220:Disulfides; D005420:Flavoproteins; D011768:Pyruvate Dehydrogenase Complex; D011994:Recombinant Proteins; D009247:NADH, NADPH Oxidoreductases; D008058:Dihydrolipoamide Dehydrogenase; D005980:Glutathione Reductase; D000123:Acetyltransferases; D051047:Dihydrolipoyllysine-Residue Acetyltransferase