Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.30.2 (endonuclease)
 18,621 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The yeast fatty acid synthase consists of two multifunctional proteins, alpha and beta, arranged in an alpha 6 beta 6 complex with a molecular weight of 2.4 x 10(6). Five of the seven enzymatic activities reside in the beta subunit, while the remaining two activities, beta-ketoacyl synthase and beta-ketoacyl reductase, and the domain of the acyl carrier protein, with its prosthetic group, 4'-phosphopantetheine, are in the alpha subunit. The genes FAS1 and FAS2 coding for beta and alpha subunits, respectively, have been cloned and the sequence of FAS1 has been reported (Chirala, S. S., Kuziora, M. A., Spector, D. M., and Wakil, S. J. (1987) J. Biol. Chem. 262, 4231-4240). In this study, we present the nucleotide sequence of the FAS2 gene. The sequence has an open reading frame, coding for a protein of 1894 amino acids with a calculated molecular weight of 207,863. The location of the serine site of attachment of the prosthetic group of the acyl carrier protein domain and the active cysteine-SH site of beta-ketoacyl synthase have been identified at residues 180 and 1312, respectively, in the deduced amino acid sequence. A putative NADPH binding site of beta-ketoacyl reductase has been suggested at residue 1038 based on the similarities to the consensus amino acid sequences -Gly-Ser-Ala- of the pyridine nucleotide enzymes. We could not find any sequence homology in the 5' flanking sequence of the FAS1 and FAS2 genes that would suggest common regulatory function. However, in the sequence of these two genes there is an identical eight-base pair sequence TCATTATG at the translational initiation site suggesting that the subunit stoichiometry probably results from equal translational efficiency of the mRNAs of both FAS1 and FAS2 genes. The S1 endonuclease mapping suggests that there is a transcriptional initiation site at about 40 nucleotides upstream of the first ATG codon and a transcriptional termination site about 300 nucleotides downstream of the TAG stop codon. The gene does not contain introns as no intron consensus TACTAAC have been found in the sequence.
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PMID:Primary structure of the multifunctional alpha subunit protein of yeast fatty acid synthase derived from FAS2 gene sequence. 290 Aug 35

Fatty acid synthetase from Saccharomyces cerevisiae is a multifunctional enzyme which catalyzes the synthesis of long chain fatty acids from acetyl- and malonyl-CoA. The enzyme is composed of two nonidentical subunits, alpha (Mr = 212,000) and beta (Mr = 203,000), which are coded for by two unlinked genes FAS2 and FAS1, respectively. Individual yeast strains containing mutations in either of the FAS genes were transformed with a bank of yeast DNA sequences in the vector YEp13. Plasmids YEpFAS1 and YEpFAS2 were selected by their ability to complement the fas1 or fas2 mutations, respectively. Additionally, we utilized an immunologic screening of a second yeast DNA bank and selected two clones 33F1 and 102B5 which produce antigenically reactive material to anti-yeast fatty acid synthetase antibodies. Through Southern hybridization experiments and restriction endonuclease mapping, a region of 5.3 kilobase pairs of 33F1 was shown to be homologous with YEpFAS1, and a span of 3.4 kilobase pairs of 102B5 was homologous with YEpFAS2. These experiments identify the yeast DNA sequences cloned into 33F1 as originating from the FAS1 gene and those DNA sequences in 102B5, from the FAS2 gene.
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PMID:Molecular cloning of fatty acid synthetase genes from Saccharomyces cerevisiae. 631 18