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Download e-book for kindle: Advances in Enzymology and Related Areas of Molecular by Alton Meister

By Alton Meister

ISBN-10: 0470123133

ISBN-13: 9780470123133

ISBN-10: 0471582794

ISBN-13: 9780471582793

Chemical and Genetic Probes of the lively 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 tools for DNA series research and Their functions within the Genome tasks (R. Wu).


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

Sample text

The former is observed as an increase in acid-stable radioactivity, and the latter is equated with a decrease in radioactivity that can be stabilized by borohydride. $- 0POse 7 %02 I H O - C - ~ ~ C O ~ ~ (I c=o I H-C-OH I H2 C - OPO 3” H:o+ 2 ‘ 4 ~ 0 ~ 0 H-;-OH I nZc- opo3m The occasional p-elimination of phosphate from the terminal carbanion of PGA to form pyruvate (74), as occurs with wild-type enzyme (1 per 125 turnovers), may offer a means of monitoring the status of the final step in catalysis.

Like the mutual exclusivity of Lys175 and Lys334 of the spinach carboxylase in their reaction with the affinity label 3(R,S)-bromo1,4-dihydroxy-2-butanone1,4-bisphosphate, the proximity of these two residues might also account for the arylation of only one or the other. The species dependence of the residue targeted could reflect differences in their relative reactivities and/or subtle differences in active-site geometries. Interestingly, both Lys329 and Lys166 in the R . rubrum enzyme are arylated by TNBS under deactivation conditions, an observation that could be interpreted to indicate that the inter-residue distance is also species dependent.

The structure of five different affinity labels for RuBP carboxylase and their primary targets within the enzyme from both spinach and R. rubrum are shown in Fig. 9. Criteria for affinity labeling that are generally fulfilled by these reagents include the following: (a) Complete inactivation as predicted when the target residue is crucial to catalysis or substrate binding. ( 6 ) Pseudo-first-order loss of activity at high molar ratios of reagent to enzyme, suggesting that inactivation correlates with the modification of a single residue.

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Advances in Enzymology and Related Areas of Molecular Biology, Volume 67 by Alton Meister

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