Evidence supporting lysine 166 of Rhodospirillum rubrum ribulosebisphosphate carboxylase as the essential base which initiates catalysis.
Open Access
- 1 May 1988
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 263 (14) , 6468-6471
- https://doi.org/10.1016/s0021-9258(18)68663-6
Abstract
No abstract availableThis publication has 21 references indexed in Scilit:
- Deuterium isotope effects in the carboxylase reaction of ribulose-1,5-bisphosphate carboxylase/oxygenaseBiochemistry, 1986
- Reaction intermediate partitioning by ribulose-bisphosphate carboxylases with differing substrate specificities.Journal of Biological Chemistry, 1986
- Kinetic mechanism of ribulosebisphosphate carboxylase: evidence for an ordered, sequential reactionBiochemistry, 1986
- An investigation of ribulosebisphosphate carboxylase activity by high resolution 1H NMRFEBS Letters, 1984
- Ribulose 1,5-bisphosphate carboxylase: fate of the tritium label in [3-3H]ribulose 1,5-bisphosphate during the enzyme-catalyzed reactionBiochemistry, 1982
- Reexamination of the binding site for pyridoxal 5'-phosphate in ribulosebisphosphate carboxylase/oxygenase from Rhodospirillum rubrumBiochemistry, 1982
- [83] Ribulosebisphosphate car☐ylase/oxygenase from Rhodospirillum rubrumPublished by Elsevier ,1982
- Characterization of the ribulosebisphosphate carboxylase-carbon dioxide-divalent cation-carboxypentitol bisphosphate complexBiochemistry, 1980
- Interaction of ribulosebisphosphate carboxylase/oxygenase with transition-state analogsBiochemistry, 1980
- d-Ribulose-1,5-bisphosphate carboxylase-oxygenaseAnalytical Biochemistry, 1977