The Regulatory Role of Muscle Pyruvate Kinase in Carbohydrate Metabolism of Invertebrates: A Comparative Study in Catalytic Properties of Enzymes Isolated from Tubifex tubifex (Oligochaeta) and Tenebrio molitor (Coleoptera)

1977 ◽  
Vol 50 (2) ◽  
pp. 142-155 ◽  
Author(s):  
Klaus-Hubert Hoffmann
2016 ◽  
Vol 406 (1-2) ◽  
pp. 231-249 ◽  
Author(s):  
Yongxing Zhu ◽  
Jia Guo ◽  
Ru Feng ◽  
Jianhua Jia ◽  
Weihua Han ◽  
...  

1972 ◽  
Vol 23 (2) ◽  
pp. 232-235 ◽  
Author(s):  
W.J.A. Van Marrewijk ◽  
D.A. Holwerda ◽  
A. De Zwaan

1975 ◽  
Vol 145 (1) ◽  
pp. 63-71 ◽  
Author(s):  
S Ainsworth ◽  
N Macfarlane

The paper reports a comparative study of the effects of Mn2+, Ni2+ and Co2+ on the reaction of ADP with phosphoenolypyruvate when catalysed by K+-activated rabbit muscle pyruvate kinase. The activation and subsequent inhibition that occurs as the bivalent ion concentration is increased is taken as evidence that the substrates of the enzyme are phosphoenolypyruvate, uncomplexed ADP and free bivalent cation. Kinetic constants for the binding of the bivalent cation to the enzyme are reported.


Sign in / Sign up

Export Citation Format

Share Document