PROTEIN DIFFERENTIATION - A COMPARISON OF ASPARTATE TRANSCARBAMOYLASE AND ORNITHINE TRANSCARBAMOYLASE FROM ESCHERICHIA-COLI K-12
PROTEIN DIFFERENTIATION - A COMPARISON OF ASPARTATE TRANSCARBAMOYLASE AND ORNITHINE TRANSCARBAMOYLASE FROM ESCHERICHIA-COLI K-12
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DOI：
10.1073/pnas.81.15.4864
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发表时间：
1984-01-01
期刊：
影响因子：
--
通讯作者：
WILD, JR
中科院分区：
文献类型：
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作者：
HOUGHTON, JE;BENCINI, DA;WILD, JR
将天冬氨酸转氨基甲酰酶(氨基甲酰磷酸：L-天冬氨酸氨基甲酰转移酶，EC 2.1.3.2)的氨基酸序列与鸟氨酸转氨基甲酰酶(氨基甲酰磷酸：L-鸟氨酸氨基甲酰转移酶，EC 2.1.3.3)的氨基酸序列进行比较。一级序列同源性为 25-40%，具体取决于同源残基的比对。同源性被纳入离散的簇中，并被长度多态性区域打断。最显着的同源性对应于推测涉及共同底物氨基甲酰磷酸结合的区域。 Chou-Fasman 预测分析表明，即使在一级序列非常不同的区域中，2 种酶内的二级结构元件也具有显着的保守性。显然，天冬氨酸转氨甲酰酶和鸟氨酸转氨甲酰酶这两种酶具有共同的进化起源，并且在其整个进化发展过程中似乎保留了相似的结构构象。
The amino acid sequence of aspartate transcarbamoylase (carbamoylphosphate:L-aspartate carbamoyltransferase, EC 2.1.3.2) was compared with that of ornithine transcarbamoylase (carbamoylphosphate:L-ornithine carbamoyltransferase, EC 2.1.3.3). The primary sequence homology is 25-40%, depending upon the alignment of homologous residues. The homologies are incorporated into discrete clusters and are interrupted by regions of length polymorphism. The most striking homologies correspond to regions putatively involved in the binding of the common substrate, carbamoyl phosphate. Chou-Fasman predictive analysis indicates substantial conservation of secondary structural elements within the 2 enzymes, even in regions whose primary sequence is quite divergent. Evidently, the 2 enzymes, aspartate transcarbamoylase and ornithine transcarbamoylase, share a common evolutionary origin and appear to have retained similar structural conformations throughout their evolutionary development.