作者: Hedvig BAHR-LINDSTROM , Hans JORNVALL
DOI: 10.1111/J.1432-1033.1984.TB08152.X
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摘要: The structural divergence between the cytoplasmic isoenzymes of aldehyde dehydrogenase from different species was investigated by analysis peptides horse protein, and correlation results with complete primary structure human isoenzyme. amino acid sequences these two proteins show a high degree homology (91% residues compared are identical). differences observed spread over entire polypeptide chains, only one cluster, which is close to reactive cysteine residue also adjacent most conserved region (covering 68 residues) in structures whole enzymes. secondary predicted for isoenzyme mainly unaffected isoenzyme, although limited conformational changes might be compatible an unexpected overrepresentation involving isoleucine (12 43 exchanges represent loss He protein). Two that correlate catalytic activity identically positioned enzyme species.