By Alton Meister
Chemical and Genetic Probes of the lively 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 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 tools for DNA series research and Their purposes within the Genome initiatives (R. Wu).
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Additional resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 67
A carboxylase mutant could enhance the rate of the nonenzymic reaction by orders of magnitude but yet appear devoid of carboxylase activity. The possibility that the detrimental consequences are due to a subtle, localized reorientation of catalytic groups cannot be rigorously excluded without high-resolution X-ray crystallographic analysis. This shortcoming can be ameliorated by the independent analysis of the competence of a mutant in catalyzing one or more of the discrete partial reactions illustrated in Fig.
The crystallographers conclude that the €-amino group is positioned whereby it could assist Mg2+ in polarizing the carbonyl of substrate (84). Catalytic properties of the K166G mutant in partial reactions argue strongly for some critical role of Lys166 in enolization, but do not allow a distinction between its serving as a general base or as a general acid. The pH profile of kcat shows that a catalytic group required for enolization must be unprotonated, a finding that would normally signal participation as a general base and exclude a role in carbonyl polarization.
10). For example, the virtually inactive K258AZmutant of aspartate aminotransferase is stimThe single-letter code is used to describe mutant proteins. The first letter denotes the amino acid present in the wild-type enzyme at the numbered position. The final letter denotes the amino acid present at the corresponding position in the mutant protein. 38 FRED C. HARTMAN AND MARK R. HARPEL Wild type mutant Lys 258 Ala 258 PY Figure 10. Illustration of noncovalent chemical rescue of a catalytically deficient mutant of aspartate aminotransferase.
Advances in Enzymology and Related Areas of Molecular Biology, Volume 67 by Alton Meister