Cloning and sequencing of a cDNA encoding rat d-dopachrome tautomerase

• Published in: FEBS letters 1995-10, Vol.373 (3), p.203-206
• Main Authors: Zhang, Miao, Åman, Pierre, Grubb, Anders, Panagopoulos, Ioannis, Hindemith, Annika, Rosengren, Evald, Rorsman, Hans
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Blotting, Northern; cDNA cloning; Cloning, Molecular; d-Dopachrome tautomerase; DNA Primers; DNA, Complementary; Humans; Indolequinones; Indoles - metabolism; Intramolecular Oxidoreductases; Isomerases - chemistry; Isomerases - genetics; Liver - enzymology; Macrophage migration; Macrophage Migration-Inhibitory Factors - chemistry; Macrophage Migration-Inhibitory Factors - genetics; Molecular Sequence Data; Open Reading Frames - genetics; PCR; Quinones - metabolism; Rat liver; Rats; Sequence Homology, Nucleic Acid
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(95)01041-C

An enzyme which converts d-dopachrome into 5,6-dihydroxyindole has recently been isolated from rat liver. Enzymatic d-dopachrome conversion has been observed in extracts from all tissues examined of several species, including man. We have now cloned and sequenced a 628 bp long cDNA encoding the enzyme provisionally called d-dopachrome tautomerase. The cDNA was isolated by 3′ and 5′ rapid amplification and cloning of cDNA ends (RACE) from rat liver cells using degenerate oligonucleotide primers, deduced from the N-terminal peptide sequence of d-dopachrome tautomerase. The cDNA contains an open reading frame encoding 118 amino acids. Edman degradation of intact and of trypsin degraded d-dopachrome tautomerase fragments gave information on and corroborated 67% of the deduced protein sequence. A homology search in the EST database found a human cDNA encoding a peptide sharing 66% homology with the rat enzyme. The rat d-dopachrome tautomerase shares 27% homology with the rat macrophage migration inhibitory factor (MIF).