MOLECULAR-CLONING AND NUCLEOTIDE-SEQUENCE OF CDNAS ENCODING HUMAN LONG-CHAIN ACYL-COA DEHYDROGENASE AND ASSIGNMENT OF THE LOCATION OF ITS GENE (ACADL) TO CHROMOSOME-2

Long-chain acyl-CoA dehydrogenase (LCAD) catalyzes the first reaction of the mitochondrial β-oxidation of fatty acids. We isolated and sequenced three cDNA clones encoding human LCAD precursor (p). The cDNAs encompass a 2217-base region including 5, 1290, and 922 bases in the 5′-noncoding, coding, and 3′-noncoding regions, respectively, and encodes the entire pLCAD of 430 amino acids (Mr: 47,656). The N-terminus of the mature human LCAD is currently unknown, but 30 (Mr 3221) and 400 amino acids (Mr: 44,435) of the sequence are considered to constitute the leader peptide and mature protein, respectively, in analogy to its rat counterpart. Human pLCAD cDNA shares 85.3 and 83.7% identical residues with rat pLCAD cDNA at the amino acid and nucleotide levels, respectively. At the amino acid level, human pLCAD shares 30.4 to 32.7% identical residues with three other human enzymes in the acyl-CoA dehydrogenase family, sharing 57 perfectly conserved residues among them. The human pLCAD gene is assigned to chromosome 2, bands q34-q35. © 1991.