Neidle E L, Hartnett C, Bonitz S, Ornston L N
Department of Biology, Yale University, New Haven, Connecticut 06511.
J Bacteriol. 1988 Oct;170(10):4874-80. doi: 10.1128/jb.170.10.4874-4880.1988.
The DNA sequence of a 1.6-kilobase-pair SalI-KpnI Acinetobacter calcoaceticus restriction fragment carrying catA, the structural gene for catechol 1,2-dioxygenase I, was determined. The 933-nucleotide gene encodes a protein product with a deduced molecular weight of 34,351. The similarly sized Pseudomonas clcA gene encodes catechol 1,2-dioxygenase II, an enzyme with relatively broad substrate specificity and relatively low catalytic efficiency. Comparison of the catA and clcA sequences demonstrated their common ancestry and suggested that acquisitions of direct and inverted sequence repetitions of 6 to 10 base pairs were frequent events in their evolutionary divergence. The catechol 1,2-dioxygenases proved to be evolutionarily homologous with the alpha and beta subunits of Pseudomonas protocatechuate 3,4-dioxygenase, and analysis of conserved residues in the intradiol dioxygenases revealed conserved histidyl and tyrosyl residues that are probably involved in the ligation of ferric ion in their active sites.
测定了携带儿茶酚1,2 -双加氧酶I结构基因catA的1.6千碱基对的醋酸钙不动杆菌SalI - KpnI限制性片段的DNA序列。这个933个核苷酸的基因编码一种推导分子量为34351的蛋白质产物。大小相似的假单胞菌clcA基因编码儿茶酚1,2 -双加氧酶II,这是一种底物特异性相对较宽、催化效率相对较低的酶。catA和clcA序列的比较显示了它们共同的祖先关系,并表明6至10个碱基对的直接和反向序列重复的获得在它们的进化分歧中是频繁发生的事件。事实证明,儿茶酚1,2 -双加氧酶与假单胞菌原儿茶酸3,4 -双加氧酶的α和β亚基在进化上是同源的,对间二酚双加氧酶中保守残基的分析揭示了可能参与其活性位点中铁离子连接的保守组氨酸和酪氨酸残基。