Two divergent MET10 genes, one from Saccharomyces cerevisiae and one from Saccharomyces carlsbergensis, encode the alpha subunit of sulfite reductase and specify potential binding sites for FAD and NADPH.

摘要: Abstract The yeast assimilatory sulfate reductase is a complex enzyme that responsible for conversion of sulfite into sulfide. To obtain information on the nature this enzyme, we isolated and sequenced MET10 gene Saccharomyces cerevisiae divergent allele from carlsbergensis. The polypeptides deduced identically sized open reading frames (1,035 amino acids) both genes have molecular masses around 115 kDa are 88% identical to each other. transcript S. has size comparable frame transcriptionally repressed by methionine in way similar seen other MET cerevisiae. Distinct homology was found between putative MET10-encoded polypeptide flavin-interacting parts flavoprotein subunit (encoded cysJ) Escherichia coli several flavoproteins. A significant N-terminal pyruvate flavodoxin oxidoreductase nifJ) Klebsiella pneumoniae, together with lack obvious flavin mononucleotide-binding motifs acid sequence, suggests distinct type reductase.