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An engineered ribonuclease preferring phosphorothioate RNA

Publication Type:

Journal Article

Authors:

Loverix,S.; Winquist,A.; Stromberg,R.; Steyaert,J.

Source:

Volume 5, Issue 5, p.365 - 368 (1998)

URL:

PM:9586998

Keywords:

Amino Acid Substitution; analogs & derivatives; analysis; Catalysis; chemistry; Cyclic GMP; genetics; Guanosine; Hydrogen; Models; Molecular; Mutagenesis; Site-Directed; MUTANT; MUTANTS; Oxygen; Protein Engineering; Ribonucleases; RNA; Substrate Specificity

Abstract:

We used mutants of RNase T1 and the Rp isomer of a thiosubstituted substrate to determine stereospecific thioeffects on catalysis. The analysis reveals subtle structural and functional changes in the intermolecular transition state interactions. Tyr 38 contributes to catalysis through a hydrogen bond with the pro-Rp oxygen. Y38F RNase T1 prefers the Rp thiosubstituted analog over the natural phosphodiester substrate that is favored by the wild type enzyme

Notes:

DA - 19980601
IS - 1072-8368 (Print)
LA - eng
PT - Letter
PT - Research Support, Non-U.S. Gov't
RN - 0 (Thionucleotides)
RN - 38557-85-6 (guanosine 2',3'-cyclophosphorothioate)
RN - 63231-63-0 (RNA)
RN - 7665-99-8 (Cyclic GMP)
RN - EC 3.1.- (Ribonucleases)
SB - IM