Enzyme Kinetics and Mechanism, Part F: Detection and by Daniel L. Purich

Enzyme Kinetics and Mechanism, Part F: Detection and by Daniel L. Purich

By Daniel L. Purich

The significantly acclaimed laboratory regular for greater than 40 years, Methods in Enzymology is among the so much hugely revered courses within the box of biochemistry. due to the fact that 1955, every one quantity has been eagerly awaited, usually consulted, and praised through researchers and reviewers alike. Now with greater than three hundred volumes (all of them nonetheless in print), the sequence comprises a lot fabric nonetheless suitable today—truly a vital e-book for researchers in all fields of lifestyles sciences. Key positive aspects * Spectroscopic Detection of response Intermediates * Isotopic and Kenetic Detection of response Intermediates * Chemical Trapping and Inhibitor equipment for Detecting response Intermediates

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Additional info for Enzyme Kinetics and Mechanism, Part F: Detection and Characterization of Enzyme Reaction Intermediates

Example text

Walsh, Biochemistry 29, 5767 (1990). i A. E. Marolewski, K. M. Mattia, M. S. Warren, and S. J. Benkovic, Biochemistry 36, 6709 (1997). J J. L. Viladot, F. Canals, X. Batllori, and A. Planas, Biochem. J. 355, 79 (2001). k K. Y. Chun, D. A. Vinarov, and H. M. Miziorko, Biochemistry 39, 14670 (2000). C a r b o x y p e p t i d a s e A. 75-]k s t r u c t u r e 75 s h o w e d that the zinc c o o r d i n a tion n u m b e r is 5, w i t h b o n d i n g i n t e r a c t i n g w i t h t w o i m i d a z o l e N ~t n i t r o gens, t h e t w o c a r b o x y l a t e o x y g e n s o f g l u t a m a t e - 7 2 , a n d a w a t e r m o l e c u l e .

Canals, X. Batllori, and A. Planas, Biochem. J. 355, 79 (2001). k K. Y. Chun, D. A. Vinarov, and H. M. Miziorko, Biochemistry 39, 14670 (2000). C a r b o x y p e p t i d a s e A. 75-]k s t r u c t u r e 75 s h o w e d that the zinc c o o r d i n a tion n u m b e r is 5, w i t h b o n d i n g i n t e r a c t i n g w i t h t w o i m i d a z o l e N ~t n i t r o gens, t h e t w o c a r b o x y l a t e o x y g e n s o f g l u t a m a t e - 7 2 , a n d a w a t e r m o l e c u l e . 75 D. C. Rees, M.

4). 4. MALDI-TOFmass spectrademonstratingthe conversionof Stpl (m/z = 17,392 [M + H]) toacovalentphosphoenzyme(m/z = 17,471 [M + H]) at timesprecedingthe steadystate. Reproduced with permissionfrom C. T. Houston,W. P. Taylor,T. S. Widlanski, and J. P. Reilly,Anal. Chem. 72, 3311 (2000). Copyright©2000 AmericanChemical Society. 90 I I l p I • Time (NO) FIG. 5. Progress curves of Stpl catalysis, demonstrating both the burst and steady-state phases of the reaction. Phosphoenzyme formation (closed circles) was assayed by MALDI-TOF MS.

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