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在利福平存在的情况下，对T7 DNA上RNA合成起始的稳态动力学研究。

Steady state kinetic studies of initiation of RNA synthesis on T7 DNA in the presence of rifampicin.

作者信息

Smagowicz J W, Scheit K H

出版信息

Nucleic Acids Res. 1977 Nov;4(11):3863-76. doi: 10.1093/nar/4.11.3863.

DOI:10.1093/nar/4.11.3863
PMID:593891
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC343206/
Abstract

The steady state kinetics of initiation of T7 DNA transcription by RNA polymerase holo enzyme from E. coli in the presence of rifampicin and the two substrates ATP and UTP were studied. Under these conditions, the enzyme catalyzes exclusively the promotor specific synthesis of pppApU. The kinetic data are in agreement with the mechanism of a truly ordered reaction. Binding of the initiating nucleotide ATP to the transcriptional complex occurs prior to the binding of the substrate UTP. Release of pppApU is most probably the rate limitinig step. Km constants were found to be 0.6 mM for ATP and 0.31 mM for UTP, respectively. The substrate inhibition pattern indicated that the substrate site exhibits a finite affinity for incorrect nucleoside triphosphate (Ki = 2.3 mM). A similar non specific binding to the 3-OH site could not be demonstrated.

摘要

研究了在利福平以及两种底物ATP和UTP存在的情况下，大肠杆菌RNA聚合酶全酶启动T7 DNA转录的稳态动力学。在这些条件下，该酶仅催化pppApU的启动子特异性合成。动力学数据与真正有序反应的机制一致。起始核苷酸ATP与转录复合物的结合发生在底物UTP结合之前。pppApU的释放很可能是限速步骤。发现ATP的Km常数分别为0.6 mM，UTP的Km常数为0.31 mM。底物抑制模式表明底物位点对错误的核苷三磷酸具有有限的亲和力（Ki = 2.3 mM）。未证明与3'-OH位点有类似的非特异性结合。

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