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- W3146099703 abstract "多重领域蛋白质涉及 DNAreplication，修理和再结合的细菌的 DNA 连接酶。它结扎的催化作用能被划分成三 steps.Todelineate 在在结扎催化作用的主题电视的氨基酸残余的角色，指导地点的异种从 Thermus sp.TAK16D.It 在细菌的NAD~+依赖的 DNA 连接酶被构造被看四保存残余( D286 ， G287 ， V289 和 K291 )在主题 IV ， overallligation.Under 上的有的重要角色挑选周转条件， D286E 的观察的明显的率， G287A ， V289I 和 K291Rmutants 清楚地在全面结扎上在火柴和 D286E 变化的失配 nickedsubstrates.The 效果上与 WT 连接酶的相比被减少不能仅仅被归功于到 thirdstep.The G287A 变化在第二步上有主要效果。全面结扎上的 V289I 和 K291Rmutation 的效果不在第三步上，也许，另外的方面例如在结扎催化作用的连接酶蛋白质的符合构造变化，被包含。而且，上面的氨基酸替换四残余在失配 nicked 底层上是更敏感的，显示提高的结扎忠实。" @default.
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- W3146099703 date "2007-01-01" @default.
- W3146099703 modified "2023-09-29" @default.
- W3146099703 title "Mutational Analysis of Bacterial NAD^＋-dependent DNA Ligase： Role of Motif IV in Ligation Catalysis" @default.
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