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In silico design of PDHK inhibitors: From small molecules to large fluorinated compounds
Published in Tanmoy Chakraborty, Prabhat Ranjan, Anand Pandey, Computational Chemistry Methodology in Structural Biology and Materials Sciences, 2017
In this chapter, I take you through my still ongoing journey to the quest for potent PDHK inhibitors. Here, I confine myself to a part of the research work, i.e., that based on the natural physiological inhibitors of kinase activity. Thisjourney started about ten years ago, when we started work on pyruvic acid, a very important molecule in biology, since it is an essential component of the metabolism process. In our quest to understand the structure and reactivity of this molecule, we carried out several studies [13−15] on the conformational stability, properties and decarboxylation reaction of the molecule, as this is the reaction involved in the metabolism of carbohydrates. Pyruvate dehydrogenase, an enzyme responsible for metabolism, catalyzes the conversion of pyruvate to acetic acid, complexed with coenzyme-A, the entire complex being named acetyl-CoA. The pyruvate dehydrogenase enzyme is actually a complex of several different activities, called the pyruvate dehydrogenase complex (PDC) and is one of the largest multienzymes found in living cells. The decarboxylation reaction is coupled (Scheme 1) to the reduction of nicotinamide adenine dinucleotide (NAD+) $ ({\text{NAD}}^{ + } ) $ to NADH [23].
Bioalcohol and Biohydrogen Production by Hyperthermophiles
Published in Ajar Nath Yadav, Ali Asghar Rastegari, Neelam Yadav, Microbiomes of Extreme Environments, 2021
Kesen Ma, Sarah Danielle Kim, Vivian Serena Chu
The two-step pathway is present in yeast and Zymomonas species, while the three-step pathway is used by E. coli and Clostridium species. Pyruvate decarboxylase (PDC) catalyzes the non-oxidative decarboxylation of pyruvate to acetaldehyde that is reduced to ethanol by alcohol dehydrogenase (ADH). Either pyruvate ferredoxin oxidoreductase (POR) or Pyruvate formate lyase (PFL) catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA that is then reduced to acetaldehyde by a CoA-dependent aldehyde dehydrogenase (AlDH).
Bioethanol production from four abundant Indian agricultural wastes
Published in Biofuels, 2020
K. M. Harinikumar, R. L. Kudahettige-Nilsson, A. Devadas, M. Holmgren, A. Sellstedt
Enzymes such as Acetaldehyde dihydrogenase (ADH)ALDH and PDC have extensively been studied in S. cerevisae [42]. In addition, a study by Kudahettige et al. [15] showed that ALD activity followed the same pattern as ethanol fermentation in T. versicolor. However, the information for T. versicolor is lacking for ALDH and PDC. Therefore, we wanted to fill this information gap and measured the activities of the two key enzymes, ALDH and PDC, in which ALDH converts acetaldehyde to acetate, thereby deflecting acetaldehyde from ethanol production, which would have a negative effect on the efficiency. Interestingly, it was shown that ALDH activity was lowest at day 0, peaked on day 3 and then decreased to day 15 (Figure 2), a very positive result. The other central enzyme in ethanol fermentation (PDC) aids the catalysis of the non-oxidative decarboxylation of pyruvate to acetaldehyde with release of carbon dioxide [42]. It was shown that PDC activity increased as the fermentations progressed, being highest in all cases on day 15, and highest in the rice fermentation. Thus, on day 15, when ALDH activity was lowest and PDC activity highest, ethanol contents were also highest (compare Figures 1, 2 and 3).