PRIMARY SEQUENCE OF THE ESCHERICHIA-COLI FADBA OPERON, ENCODING THE FATTY ACID-OXIDIZING MULTIENZYME COMPLEX, INDICATES A HIGH DEGREE OF HOMOLOGY TO EUKARYOTIC ENZYMES
PRIMARY SEQUENCE OF THE ESCHERICHIA-COLI FADBA OPERON, ENCODING THE FATTY ACID-OXIDIZING MULTIENZYME COMPLEX, INDICATES A HIGH DEGREE OF HOMOLOGY TO EUKARYOTIC ENZYMES
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DOI：
10.1128/jb.172.11.6459-6468.1990
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发表时间：
1990-11-01
影响因子：
3.2
通讯作者：
DIRUSSO, CC
中科院分区：
文献类型：
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作者：
DIRUSSO, CC
在大肠杆菌中，脂肪酸的β-氧化所需的至少五种酶活性与由α 2 β 2构象的两个亚基组成的多酶复合物有关（A. Pramanik等人，J. Bacteriol. 137：469-473，1979）。在本工作中，已确定编码这两个亚基，fadB和fadA的基因的DNA序列。转录的方向是从fadB到fadA，而不是从fadA到fadB，如前所述（S。K. Spratt等人，J. Bacteriol. 158：535-542，1984）。这两种肽的编码序列之间只有10个核苷酸，证实了这些基因形成操纵子的建议。由fadB和fadA编码的肽的长度分别为729个氨基酸。较大和较小的肽预测分子量分别为79，678和49，876 Da。最近，fadA基因的序列发表在单独的报道中（Yang et al.，265：10424-10429，1990）。在这项工作中，确认了fadA的大部分DNA序列，并纠正了10个错误。这些核苷酸的变化导致5个氨基酸残基的变化预测在羧基末端的fadA编码的肽。通过与其它肽序列比较，α. fadB内编码的亚基与大鼠过氧化物酶体烯酰辅酶A：水合酶-3-羟酰辅酶A脱氢酶三功能酶在两种肽的全长上具有31%的完全同一性。与Yang等人的工作一致，的βfadA内编码的亚基在肽的整个长度上与来自不同真核生物来源的五个硫解酶基因具有35%至45%的完全同一性。
In Escherichia coli at least five enzyme activities required for the beta-oxidation of fatty acids are associated with a multienzyme complex composed of two subunits in .alpha.2.beta.2 conformation (A. Pramanik et al., J. Bacteriol. 137:469-473, 1979). In the present work, the DNA sequence of the genes encoding these two subunits, fadB and fadA, has been determined. The direction of transcription was from fadB to fadA rather than from fadA to fadB, as suggested previously (S. K. Spratt et al., J. Bacteriol. 158: 535-542, 1984). Only 10 nucleotides separated the coding sequences for the two peptides, confirming the suggestion that these genes form an operon. The peptides encoded by fadB and fadA were 729 amino acids, respectively, in length. The larger and smaller peptides had predicted molecular masses of 79,678 and 49,876 Da, respectively. Recently, the sequence of the fadA gene was published in a separate report (Yang et al., J. Biol. Chem. 265:10424-10429, 1990). In this work, most of the DNA sequence for fadA was confirmed, and 10 errors were corrected. Three of these nucleotide changes resulted in five amino acid residue changes predicted in the carboxy terminus of the fadA-encoded peptide. By comparison to other peptide sequences, the .alpha. subunit encoded within fadB had 31% perfect identity with the rat peroxisomal enoyl-coenzyme A:hydratase-3-hydroxyacyl-coenzyme A dehydrogenase trifunctional enzyme over the entire length of the two peptides. In agreement with the work of Yang et al., the .beta. subunit encoded within fadA had 35 to 45% perfect identity with five thiolase genes from different eucaryotic sources over the entire length of the peptide.