By Alton Meister
Chemical and Genetic Probes of the energetic website of D-Ribulose-1,5-Bifphosphate Carboxylase/Oxygenase: A Retrospective in keeping with the third-dimensional constitution (F. Hartman & M. Harpel).
Phenylalanine Hydroxylating process (S. Kaufman).
Post-Translational amendment of Proteins (R. Krishna & F. Wold).
The position 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 purposes within the Genome tasks (R. Wu).
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Additional info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 67
2,4,6-Trinitrobenzenesulfonate(TNBS) proves to be an ideal reagent for this purpose due to its selectivity for Lys166 of the R. rubrum enzyme and Lys334 of the spinach enzyme (115). The reaction of TNBS with amines is second-order, and the pHdependences of rates show that only unprotonated amino groups are reactive (116, 117). The observed second-order rate constant ( k 2 ) will then reflect the degree of ionization. The calculated pK, values and intrinsic reactivities (k,) of the unprotonated amino group of acetyllysine, Lys166 of the activated R.
Treatment of the complex with diazomethane yields an esterified carbamate that is sufficiently stable to survive proteolysis and peptide fractionation. Although the esterification is random, only the site of interest is tagged with radioactivity (100, 101). The proximity of the Mg2+ ion to the carbamate carbon and the bound CABP, as deduced from NMR and EPR, led to the conclusions that the activator lysyl residue is an integral component of the active site and that the enzyme does not contain separate sites for activation and catalysis (95).
The P/(Y barrel domain of the active site is illustrated by the rectangular indentations, and the Nterminal domain of the active site is illustrated by the triangular indentations. Indentations outlined in black represent nonfunctional domains due to specific amino acid substitutions. Heterodimer formation from the two mutant subunits generates a species with one catalytically functional active site per dimeric molecule. 50 FRED C. HARTMAN AND MARK R. HARPEL mains, functional analyses would still have been required to verify a direct role of N-terminal residues in catalysis.