BIOCHEMICAL-CHARACTERIZATION OF ESCHERICHIA-COLI DNA HELICASE-I
BIOCHEMICAL-CHARACTERIZATION OF ESCHERICHIA-COLI DNA HELICASE-I
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DOI：
10.1111/j.1365-2958.1992.tb01555.x
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发表时间：
1992-05-01
影响因子：
3.6
通讯作者：
MINKLEY, EG
中科院分区：
文献类型：
--
作者：
DASH, PK;TRAXLER, BA;MINKLEY, EG
F tral的基因产物是一种双功能蛋白，在接合DNA转移过程中切割和解旋F质粒。对Tral蛋白的进一步生化表征表明，除了之前确定的K（m）之外，它还具有第二个（低得多）的ATP水解K（m）。单链DNA刺激的ATP酶速率的测量表明，酶单体之间存在合作相互作用以获得最大活性。此外，O-18-交换交换实验表明，Tral蛋白水解ATP，最多，在每个营业额的水解步骤的低水平逆转。
The gene product of F tral is a bifunctional protein which nicks and unwinds the F plasmid during conjugal DNA transfer. Further biochemical characterization of the Tral protein reveals that it has a second, much lower, K(m) for ATP hydrolysis, in addition to that previously identified. Measurement of the single-stranded DNA-stimulated ATPase rate indicates that there is co-operative interaction between the enzyme monomers for maximal activity. Furthermore, O-18-exchange exchange experiments indicate that Tral protein hydrolyses ATP with, at most, a low-level reversal of the hydrolytic step during each turnover.