Determination of the nucleotide conformation in the productive enzyme-substrate complexes of RNA-depolymerases

The aim of this work is to determine the conformation of the nucleobase adjacent to the cleavable phosphodiester bond in the productive enzyme-substrate complex of RNA-depolymerizing enzymes. To this end the kinetic parameters of hydrolysis of UpA, 2′-C-Me- and 3′-C-Me-UpA were determined for RNase...

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Veröffentlicht in:	FEBS letters 1997-03, Vol.404 (2), p.169-172
Hauptverfasser:	Moiseyev, G.P, Yakovlev, G.I, Lysov, Yu.P, Chernyi, A.A, Polyakov, K.M, Oivanen, M, Lönnberg, H, Beigelman, L.N, Efimtseva, E.V, Mikhailov, S.N
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Calorimetry Cattle Conformation of substrate C′-methyl analogues of UpA Dinucleoside Phosphates - chemistry Dinucleoside Phosphates - metabolism Nucleic Acid Conformation Penicillium - enzymology Phosphoric Diester Hydrolases - chemistry Phosphoric Diester Hydrolases - metabolism Protein Conformation Ribonuclease, Pancreatic - chemistry Ribonuclease, Pancreatic - metabolism Ribonucleases - chemistry Ribonucleases - metabolism RNA-depolymerizing enzyme Single-Strand Specific DNA and RNA Endonucleases - chemistry Single-Strand Specific DNA and RNA Endonucleases - metabolism Snake Venoms
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