HUMAN SHORT-CHAIN L-3-HYDROXYACYL-COA DEHYDROGENASE - CLONING AND CHARACTERIZATION OF THE CODING SEQUENCE

The cDNA encompassing the complete coding sequence of human liver shor t-chain L-3-hydroxyacyl-CoA dehydrogenase (SCHAD) was isolated and cha racterized. Screening of a cDNA library combined with rapid amplificat ion of 5' cDNA ends resulted in a SCHAD cDNA sequence of 1877 bp. It e ncodes a protein of 314 amino acids with a calculated molecular weight of 34,3 kDa. containing a mitochondrial import signal peptide of 12 a mino acids and 302 amino acids of mature SCHAD protein, The deduced am ino acid sequence of the mature protein shows a 92 percent identity wi th SCHAD from pig heart. Northern blot analysis reveals SCHAD mRNA to be expressed in liver, kidney, pancreas, heart and skeletal muscle. Th e human SCHAD gene was mapped by fluorescence in situ hybridization to chromosome 4q22-26. (C) 1996 Academic Press, Inc.