scholarly journals Slow Conformational Changes of the Inorganic Pyrophosphatase from Bakers' Yeast Induced by Divalent Metal Ions

1973 ◽  
Vol 33 (2) ◽  
pp. 323-331 ◽  
Author(s):  
Wolsfgang E. Hohne ◽  
Tom A. Rapoport
1980 ◽  
Vol 58 (3) ◽  
pp. 188-193 ◽  
Author(s):  
Chiu-Yin Kwan ◽  
Robert C. Davis

The interactions of L-Phe and L-Ala with rabbit muscle pyruvate kinase depended upon the nature of divalent metal ions studied: Mg(II), Co(II), Mn(II), and Ni(II). L-Phe inhibited all metal derivatives of the enzyme except Mn(II)–enzyme. L-Ala inhibited only Ni(II)–enzyme and had no effect on other metal derivatives. The inhibition by L-Phe could be partially or completely reversed by L-Ala for all metal derivatives. The mode of inhibition of pyruvate kinase by L-Phe depended upon pH as well as the nature of activating divalent metal ions. The sigmoidal response increased with increasing pH for all metal derivatives inhibited by L-Phe. L-Phe and L-Ala strongly perturbed the coordination sphere of enzyme bound Co(II), but not Ni(II). There were poor correlations between visible circular dichroic (cd) spectral changes and the corresponding kinetic changes. However, L-Phe and (or) L-Ala induced ultraviolet cd and difference absorption spectral changes, on the other hand, corresponded remarkably well with the kinetic observations.


2017 ◽  
Vol 15 (41) ◽  
pp. 8802-8809 ◽  
Author(s):  
Alessio Peracchi ◽  
Maria Bonaccio ◽  
Alfredo Credali

Placing 2-aminopurine at position 15 of the 8–17 DNAzyme allows the detection of a specific metal-induced conformational change, apparently coupled to the activation of catalysis.


Biochemistry ◽  
2015 ◽  
Vol 54 (41) ◽  
pp. 6369-6381 ◽  
Author(s):  
Aamir Mir ◽  
Ji Chen ◽  
Kyle Robinson ◽  
Emma Lendy ◽  
Jaclyn Goodman ◽  
...  

1991 ◽  
Vol 81 (4) ◽  
pp. 462-466 ◽  
Author(s):  
Maria Fabiana Drincovich ◽  
Alberto A. Iglesias ◽  
Carlos S. Andreo

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