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.
Nakanishi
M
M
Laboratory of Biochemistry, Gifu Pharmaceutical University, Japan.
Deyashiki
Y
Y
Nakayama
T
T
Sato
K
K
Hara
A
A
D000429:Alcohol Oxidoreductases / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D008168:Lung / Q000201:enzymology*; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000235:genetics*; D011506:Proteins / Q000235:genetics; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D013552:Swine
D011506:Proteins; D010088:Oxidoreductases; D000429:Alcohol Oxidoreductases; C082627:pig lung carbonyl reductase; C082628:Cbr2 protein, mouse