CONSERVED DOMAINS IN MOLYBDENUM HYDROXYLASES - THE AMINO-ACID SEQUENCE OF CHICKEN HEPATIC SULFITE OXIDASE
- 15 December 1989
- journal article
- research article
- Vol. 264 (35) , 20894-20901
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, R. (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 sequences forming the molybdenum-binding domains of the molybdenum hydroxylases may have evolved from a common ancestral gene.This publication has 10 references indexed in Scilit:
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