Conway T, Ingram L O
School of Biological Sciences, University of Nebraska, Lincoln 68588-0118.
J Bacteriol. 1989 Jul;171(7):3754-9. doi: 10.1128/jb.171.7.3754-3759.1989.
The gene that encodes 1,2-propanediol oxidoreductase (fucO) from Escherichia coli was sequenced. The reading frame specified a protein of 383 amino acids (including the N-terminal methionine), with an aggregate molecular weight of 40,642. The induction of fucO transcription, which occurred in the presence of fucose, was confirmed by Northern blot analysis. In E. coli, the primary fucO transcript was approximately 2.1 kilobases in length. The 5' end of the transcript began more than 0.7 kilobase upstream of the fucO start codon within or beyond the fucA gene. Propanediol oxidoreductase exhibited 41.7% identity with the iron-containing alcohol dehydrogenase II from Zymomonas mobilis and 39.5% identity with ADH4 from Saccharomyces cerevisiae. These three proteins did not share homology with either short-chain or long-chain zinc-containing alcohol dehydrogenase enzymes. We propose that these three unusual alcohol dehydrogenases define a new family of enzymes.
对来自大肠杆菌的编码1,2 - 丙二醇氧化还原酶（fucO）的基因进行了测序。该阅读框编码一个由383个氨基酸组成的蛋白质（包括N端甲硫氨酸），总分子量为40,642。通过Northern印迹分析证实，在岩藻糖存在的情况下会发生fucO转录的诱导。在大肠杆菌中，fucO初级转录本长度约为2.1千碱基。转录本的5'端起始于fucA基因内部或其之外、fucO起始密码子上游超过0.7千碱基处。丙二醇氧化还原酶与运动发酵单胞菌的含铁乙醇脱氢酶II有41.7%的同一性，与酿酒酵母的ADH4有39.5%的同一性。这三种蛋白质与含锌的短链或长链乙醇脱氢酶均无同源性。我们提出这三种不同寻常的乙醇脱氢酶定义了一个新的酶家族。
