scholarly journals Deficiency in a Very-Long-Chain Fatty Acid β-Ketoacyl-Coenzyme A Synthase of Tomato Impairs Microgametogenesis and Causes Floral Organ Fusion

2012 ◽  
Vol 161 (1) ◽  
pp. 196-209 ◽  
Author(s):  
Anna Smirnova ◽  
Jana Leide ◽  
Markus Riederer
1980 ◽  
Vol 26 (8) ◽  
pp. 863-873 ◽  
Author(s):  
Anthony F. Cacciapuoti ◽  
Stephen A. Morse

The glucose-6-phosphate dehydrogenase from Neisseria gonorrhoeae was inhibited by long-chain fatty acid acyl-coenzyme A derivatives. The inhibition was increased at low concentrations of glucose 6-phosphate and was greater with the NAD-linked activity (ca. 0.05 mM inhibitor required for 50% inhibition) than with the NADP-linked activity (ca. 0.2 mM required for 50% inhibition). Bovine serum albumin and spermine could prevent the inhibition by the acyl-coenzyme A derivatives, but neither of these compounds nor high concentrations of cofactors or substrate could reverse the effect. Dilution of enzyme–inhibitor preincubation mixtures appeared to reverse the inhibition. The inhibition by stearoyl-coenzyme A was of the mixed type, and the inhibitor appeared to have a greater affinity for the free enzyme (Ki = 0.016–0.05 mM) than for enzyme bound to cofactor or substrate (Kis = 0.07–0.08 mM). Glucose-6-phosphate dehydrogenase activity was also inhibited competitively by adenosine 5′-triphosphate and was strongly regulated by adenylate energy charge values between 0.9 and 1.0. Kinetic and other characteristics of the enzyme are presented, and the possible role of glucose-6-phosphate dehydrogenase as a target for fatty acid toxicity in gonococci, mediated in the form of the acyl-coenzyme A derivatives, is discussed.


2000 ◽  
Vol 41 (1) ◽  
pp. 41-47 ◽  
Author(s):  
Karin A. J.M. van der Lee ◽  
Michaël M. Vork ◽  
Johan E. De Vries ◽  
Peter H.M. Willemsen ◽  
Jan F.C. Glatz ◽  
...  

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