| Literature DB >> 16664961 |
J Pierce1.
Abstract
Recent studies have provided a fairly detailed view of the various intermediates involved in the reactions of ribulosebisphosphate carboxylase and the manner in which the catalytically essential metal atom might catalyze their interconversions. A better understanding of how the enzyme distinguishes between its alternate substrates, CO(2) and O(2), has also emerged. The results of these studies should prove useful in anticipating possible ways in which the enzyme's substrate specificity might be manipulated. Together, the techniques that are described constitute a powerful methodology for more refined experimentation aimed at understanding the curious reactivities of ribulosebisphosphate carboxylase.Entities:
Year: 1986 PMID: 16664961 PMCID: PMC1075463 DOI: 10.1104/pp.81.4.943
Source DB: PubMed Journal: Plant Physiol ISSN: 0032-0889 Impact factor: 8.340