By Alton Meister
Ribonuclease P: An Enzyme with a Catalytic RNA Subunit (S. Altman).
rules of Escherichia coli Glutamine Synthetase (S. Rhee, et al.).
Glucose 6-Phosphatase: options of Membrane-Function courting (K. Sukalski & R. Nordlie).
Chiral Phosphorothioates: Stereochemical research of Enzymatic Substitution at Phosphorus (P. Frey).
Serotonin and Peptide Immunoneuromodulators: contemporary Discoveries and New principles (D. Silverman & M. Karnovsky).
The Phosphyglycerate Mutases (L. Fothergill-Gilmore & H. Watson).
Mechanism and law of the Glutamine-Dependent Carbamyl Phosphate Synthetase of Escherichia coli (A. Meister).
Cummulative Index, Vols.
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Additional resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 62
26 RIBONUCLEASE P 27 (63,64) (Fig. 7). The ability of these intron derivatives to function as an endonucleases and as “replicases” has important implications for the evolution of early biochemical systems. Cech’s results lend added weight to the hypothesis that these early systems could have utilized RNA exclusively as the genetic and enzymatic material. B. COMPARISONS One indication of the differences in the mechanisms catalyzed by RNAs is the nature of the end groups generated during the cleavage of phosphoester bonds.
2 and at 37°C. This binding is accompanied by a rapid release 48 S. RHEE, P. CHOCK AND E. STADTMAN of two H per subunit, and Mn(I1) competitively displaces the bound Co(I1) (57). However, the ultraviolet absorption spectrum changes due to Co(I1) binding at the nl site are distinctly different from that of Mn(II), and the time course for this Co(I1)-inducedoptical density change is also slower. The catalytic properties of the Co(I1)-activated enzyme are different from the Mg(I1)-supported form with respect to its V,,,,,, K,, pH-activity profile, and sensitivity toward feedback inhibitors (54).
By contrast, the reactions that produce a 5’-phosphate group in their cleavage products must do so by mechanisms that differ in some details from, ~ but may have a lot in common with, the well-studied S N in-line ~ which displacement reaction (35). The variation of the S N reaction has been proposed as an explanation of the RNase P reaction is shown in Fig. 8. The difference from the standard S N ~reaction P Figure 8. Hypothetical electronic mechanism of tRNA precursor hydrolysis by MI RNA of RNase P.
Advances in Enzymology and Related Areas of Molecular Biology, Volume 62 by Alton Meister