By Alton Meister
Chemical and Genetic Probes of the energetic web site of D-Ribulose-1,5-Bifphosphate Carboxylase/Oxygenase: A Retrospective according to the third-dimensional constitution (F. Hartman & M. Harpel).
Phenylalanine Hydroxylating process (S. Kaufman).
Post-Translational amendment of Proteins (R. Krishna & F. Wold).
The function of steel Clusters and MgATP in Nitrogenase Catalysis (L. Mortenson, et al.).
Myristoyl CoA: Protein N-Myristoyl-Transferase (D. Rudnick, et al.).
improvement of Enzyme-Based equipment for DNA series research and Their functions within the Genome initiatives (R. Wu).
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Extra info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 67
Despite the more stringent requirements for coexpression of two genes and for proper assembly of their encoded dissimilar polypeptides, expression systems for L8S8 enzymes have also been described, thereby enabling appli- 34 FRED C. HARTMAN AND MARK R. HARPEL cation of site-directed mutagenesis to questions of assembly and function of S subunits (122- 126). The maximal potential of site-directed mutagenesis in establishing structure-function correlations can only be realized in those cases in which the three-dimensional structures of both the native protein and pertinent mutant proteins have been elucidated.
The reaction-intermediate analog CABP offers a convenient and powerful tool for ascertaining if an inactive mutant can nevertheless CHEMICAL AND GENETIC PROBES OF RUBISCO 35 form a carbamate and bind phosphorylated ligands. Only the activated form of the wild-type enzyme binds the analog with sufficient tenacity to form a stable quaternary complex comprised of equimolar amounts of enzyme subunit, COz, Mg”, and CABP. This complex is readily isolated by gel filtration (127). Its stability is emphasized by a consideration of the exchange rates between bound ligand and excess free ligand added to the complex: t112 ( R .
In the former case, the K166G mutant should retain activity with XuBP as substrate, whereas the latter predicts parallel abolishment of carboxylation activity with both RuBP and XuBP. In preliminary experiments, CHEMICAL AND GENETIC PROBES OF RUBISCO 53 K166G appears incapable of catalyzing XuBP turnover (E. H. Lee and F. C. Hartman, unpublished). If the exclusion of Lys166 on structural grounds as the acceptor of the C3 proton of RuBP is correct, what functional group then is the base? As mentioned earlier, a number of alternative candidates have been put forward based on several crystal structures at various stages of refinement.
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