A Two-Binding-Site Kinetic Model for the Ribonuclease-T1-Catalysed Transesterification of Dinucleoside Phosphate Substrates
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1995.140_1.x/fullpdf
Reference36 articles.
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3. Zum Mechanismus der Ribonuclease-Reaktion. 2. Die Vorordnung im Substrat als geschwindigkeitssteigernder Faktor bei Dinucleosidphosphaten und analogen Verbindungen
4. Identification by site-directed mutagenesis of amino acids in the subsite of bovine pancreatic ribonuclease A
5. The structural and sequence homology of a family of microbial ribonucleases
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2. RNase-Stable RNA: Conformational Parameters of the Nucleic Acid Backbone for Binding to RNase T1;Biological Chemistry;2001-01-20
3. Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallograph;Nature Structural Biology;1998-04
4. A Decade of Protein Engineering on Ribonuclease T1- Atomic Dissection of the Enzyme-Substrate Interactions;European Journal of Biochemistry;1997-07
5. Upstream subsite interactions for oligonucleotide binding with ribonuclease T1;Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression;1997-02
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