Human fatty acid synthase: properties and molecular cloning.

• DOI: 10.1073/pnas.92.19.8695
• Publication Date: 2006-05-31T13:19:27Z
• Authors: A Jayakumar; M H Tai; W Y Huang; W al-Feel; M Hsu; L Abu-Elheiga; S S Chirala; S J Wakil
• Keywords: 2. Zero hunger; 0303 health sciences; Carcinoma, Hepatocellular; DNA, Complementary; Base Sequence; Sequence Homology, Amino Acid; Liver Neoplasms; Molecular Sequence Data; Restriction Mapping; Brain; Sequence Analysis, DNA; Rats; 03 medical and health sciences; Species Specificity; Pantetheine; Tumor Cells, Cultured; Animals; Humans; Tissue Distribution; Amino Acid Sequence; Cloning, Molecular; Fatty Acid Synthases; Chickens

Fatty acid synthase (FAS; EC 2.3.1.85) was purified to near homogeneity from a human hepatoma cell line, HepG2. The HepG2 FAS has specific activity of 600 nmol NADPH oxidized per min mg, which is about half that chicken liver FAS. All the partial activities are comparable those other animal FASs, except for beta-ketoacyl synthase, whose significantly lower attributable low 4'-phosphopantetheine content We cloned brain cDNA. cDNA sequence an open reading frame 7512 bp encodes 2504 amino acids (M(r), 272,516). 79% and 63% identity, respectively, with sequences rat enzymes. Northern analysis revealed mRNA 9.3 kb in size its level varied among tissues, brain, lung, tissues showing prominent expression. nucleotide segment (bases 2327-3964) identical normal 53-bp 3892-3944) does not alter frame. This altered also present genomic DNA. origin significance this variance gene unclear, but apparently contribute