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    Biochem Biophys Res Commun. 1991 Oct 31;180(2):887-93.

    Cloning and sequence analysis of the human liver rhodanese: comparison with the bovine and chicken enzymes.

    Pallini R, Guazzi GC, Cannella C, Cacace MG.

    Source

    Istituto di Scienze Neurologiche, Fac. Med. Chir., Università di Siena, Italy.

    Abstract

    The cDNA for the human rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1), a nuclearly encoded protein of the mitochondrial matrix, was isolated from a human fetal liver cDNA library. Nucleotide sequence revealed an open reading frame coding for a polypeptide of 295 amino acids, which presented a 57% and 58% identity with the bovine and avian rhodanese, respectively. The analysis of the 5'-ends of the coding region gave no evidence for the presence of a cleavable signal sequence as found in other mitochondrial proteins. A comparison with two available amino acid sequences (cow and chicken) showed that sequence similarity is not restricted to the alpha-helices and beta-structures motifs which are remarkably superimposable in the two halves of bovine rhodanese, but extends to adjacent regions.

    PMID:
    1953758
    [PubMed - indexed for MEDLINE]

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