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- W768735852 abstract "This chapter focuses on mechanistic issues involved in RNA-modifying enzymes. From a chemical/structural viewpoint, modified nucleosides can be divided into two groups. The first group consists of relatively “simple” modifications (e.g., methylation, thiolation, deamination, and isomerization). The second group of modified nucleosides consists of more “complex” modifications (e.g., multiple modifications and hypermodifications), involving a multi-enzyme pathway or, as is the case with queuine and archaeosine, involving biosynthetic precursors synthesized by other enzymes for this purpose alone. The X-ray crystal structure of a nucleoside adenosine deaminase has been determined, and a zinc ion and an ordered water molecule have been located in the active site. The X-ray crystal structure of cytidine deaminase complexed with uridine has also recently been determined. The miaA enzyme utilizes Δ2-isopentenyl pyrophosphate (IPP, or dimethylallyl diphosphate) as the isopentenyl group donor. Δ2-IsopentenyI pyrophosphate is utilized by a number of isopentenyl transferases leading to various isoprenoids and ultimately to steroids. Two reaction mechanisms have been postulated for the isopentenyl transferases, an associative mechanism and a dissociative mechanism. Technological advances in RNA generation (both by in vitro transcription and by chemical synthesis) along with advances in molecular biological approaches (to identify, clone and express modifying enzyme genes) have been predominantly responsible for the renewed activity in RNA modification and editing research." @default.
- W768735852 created "2016-06-24" @default.
- W768735852 creator A5021260291 @default.
- W768735852 creator A5068404284 @default.
- W768735852 date "2014-04-30" @default.
- W768735852 modified "2023-10-17" @default.
- W768735852 title "Mechanisms of RNA-Modifying and -Editing Enzymes" @default.
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