Cloning and sequence analysis of a cDNA encoding tetrameric carbonyl reductase of pig lung

A cDNA for tetrameric carbonyl reductase was cloned from a pig lung cDNA library. The cDNA had an open reading frame encoding a protein of 244 amino acid residues with a predicted monomer molecular weight of 25,985. The authenticity of the cDNA was confirmed by a perfect match of 80 amino acids determined from sequencing of amino-terminus, carboxy-terminus and internal fragments of the purified enzyme. The deduced sequence of the carbonyl reductase shows a similarity to those of the short-chain alcohol dehydrogenase superfamily proteins; notably it had an extensive homology (85% identical residues) with a putative gene product of murine adipocyte.