The substrate reactivity of .mu.-monothiopyrophosphate with pyrophosphate-dependent phosphofructokinase: evidence for a dissociative transition state in enzymic phosphoryl group transfer
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00106a032
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1. μ-Monothiopyrophosphate as a Substrate for Inorganic Pyrophosphatase and UDP-Glucose Pyrophosphorylase;Archives of Biochemistry and Biophysics;1996-11
2. Kinetic and Thermodynamic Characterization of the Reaction Catalyzed by a Polynucleotide Kinase Ribozyme;Biochemistry;1995-11
3. Errors and artifacts in coupled spectrophotometric assays of enzyme activity;Phytochemistry;1995-03
4. An expedient synthesis of symmetrical tetra-alkyl monothiopyrophosphates;Tetrahedron Letters;1994-08
5. Lanthanide Pyrophosphates as Substrates for the Pyrophosphate-Dependent Phosphofructokinases from Propionibacterium freudenreichii and Phaseolus aureus: Evidence for a Second Metal Ion Required for Reaction;Biochemistry;1994-02-22
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