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By Alton Meister

Chemical and Genetic Probes of the energetic website of D-Ribulose-1,5-Bifphosphate Carboxylase/Oxygenase: A Retrospective according to the three-d constitution (F. Hartman & M. Harpel).

Phenylalanine Hydroxylating method (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 tasks (R. Wu).


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Additional info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 67

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These experiments document that the formation of the enediol(ate) at the active site, though a prerequisite for overall catalysis, is insufficient for completion of the catalytic cycle. These experiments also provide the first direct evidence that the enzyme plays an active, indispensable role in facilitating the attack of COz or O2 on the enediol(ate). Given the Theorell-Chance mechanism of Rubisco, this step could have been viewed as noncatalytic. However, presteady-state kinetics have invoked a partially rate-determining step between the enediol(ate) and its reaction with COz (28), so a direct role of Lys329 in activation of the ene- 46 FRED C.

However, this tenet is complicated by the finding based on NMR that the activator within the complex is bicarbonate, not COz (S. Gutteridge and G. H. Lorimer, personal communication). Presumably, bicarbonate engages the sulfhydryl of Cys 191 through H-bonding, which properly juxtaposes the oxyanion as a ligand for Mg2+. If bicarbonate can H-bond with the sulfhydryl of Cysl91, so should numerous other compounds. The question then posed was whether a primary amine, which possesses a H-bonding functional group, could revive the inactive K191C mutant.

More recently, in vitro hybridization of catalytically deficient Rubisco mutants have been used to clarify the folding process as promoted by chaperonins (156). Additional questions concerning subunit-subunit interactions may also be approached via hybridization of site-directed mutant proteins. Replacement of Lys166 with Asp (119) or Lys168 with Glu (157) precluded the formation of stable dimeric proteins. The former finding prompted the suggestion that electrostatic repulsion between the newly introduced negative charge at position 166 and nearby negative charges in the NHz-terminal domain of the adjacent subunit were responsible for interference in subunit-subunit association.

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