title: Conserved domains in molybdenum hydroxylases. The amino acid sequence of chicken hepatic sulfite oxidase.
abstract: The amino acid sequence of the molybdenum-containing domain of chicken hepatic sulfite oxidase has been determined by Edman degradation of the purified protein. Combining these data with those previously published for the heme-containing domain (Guiard, B., and Lederer, F. (1979) Eur. J. Biochem. 100, 441-453) indicates that each subunit of the homodimer comprises a single polypeptide chain containing 460 amino acid residues (Mr = 50,545). Comparison of the sequence with the cDNA-deduced sequence of assimilatory nitrate reductase from Arabidopsis thaliana shows a substantial degree of sequence conservation in the regions of the proteins that have been identified as comprising the Mo-pterin- and cytochrome b557-binding domains. These results suggest that the sequences forming the molybdenum-binding domains of the molybdenum hydroxylases may have evolved from a common ancestral gene.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of South Florida, College of Medicine, Tampa.
authors.forename: P J
authors.initials: PJ
authors.lastname: Neame
authors.forename: M J
authors.initials: MJ
authors.lastname: Barber
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D008099:Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D008982:Molybdenum / Q000378:metabolism*; D009565:Nitrate Reductases / Q000235:genetics*; D010088:Oxidoreductases / Q000235:genetics*; D050862:Oxidoreductases Acting on Sulfur Group Donors / Q000235:genetics*; D010446:Peptide Fragments / Q000302:isolation & purification; D010447:Peptide Hydrolases; D010944:Plants / Q000201:enzymology / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid
chemical_list: D010446:Peptide Fragments; D008982:Molybdenum; D010088:Oxidoreductases; D009565:Nitrate Reductases; D050862:Oxidoreductases Acting on Sulfur Group Donors; D010447:Peptide Hydrolases