EC Number |
General Information |
Reference |
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2.3.1.54 | metabolism |
anaerobic fermentation pathway yielding 3 ATP per glucose, pyruvate channeling to fermentation product, lactate dehydrogenase and pyruvate dehydrogenase are alternative pyruvate channeling enzymes during fermentation |
701826 |
2.3.1.54 | metabolism |
anaerobic glucose metabolism, direct link between fermentative metabolism and virulence in infected mice |
704002 |
2.3.1.54 | physiological function |
enzyme deletion mutant displays pleiotropic effects. In the mutant, no formate is produced, glucose consumption is delayed, and ethanol production is decreased, whereas acetate and lactate production are unaffected. All metabolic alterations can be restored by addition of formate or complementation of the mutant. In compensation reactions, serine and threonine are consumed better by the mutant than by the wild-type. The mutant displays reduced production of formylated peptides compared to the parental strain. Arginine consumption and arc operon transcription are increased in the mutant. Enzyme plays a significant role in the anaerobic layer of a biofilm |
719737 |
2.3.1.54 | metabolism |
the enzyme takes part in the metabolic pathway of pyruvate to ethanol in Thermoanaerobacterium saccharolyticum |
-, 735819 |
2.3.1.54 | physiological function |
the physiological role of pyruvate formate-lyase is supplying C1 units for biosyntheses |
-, 735819 |
2.3.1.54 | physiological function |
anaerobic alkane degradation in Archaeoglobus fulgidus may involve the gene pflD in alkane activation through addition to fumarate |
736285 |
2.3.1.54 | metabolism |
NADH generated from anaerobic glycerol metabolism in the absence of fumarate is oxidized through the pyruvate formate-lyase-ethanol fermentation pathway. Thus, the enzyme is essential to avoid the accumulation of excess NADH during fumarate-independent anaerobic glycerol metabolism |
-, 736361 |
2.3.1.54 | physiological function |
enzyme pyruvate formate-lyase is responsible for intracellular formate generation in enterobacteria and other microbes |
736638 |
2.3.1.54 | physiological function |
pyruvate formate lyase (PFL) forms an alternative pathway for acetyl-CoA biosynthesis. Pyruvate formate lyase is characterized as an enzyme functional at anaerobic conditions, since the radical in the enzyme's active form is sensitive to oxygen. PFL pathway can be functional at aerobic growth conditions in yeast when coexpressed with appropriate electron donors |
744943 |
2.3.1.54 | physiological function |
pyruvate formate-lyase (PFL) supplies the citric acid cycle with acetyl-CoA during anaerobic glycolysis by catalyzing the formation of acetyl-CoA and formate from CoA and pyruvate, and is a central enzyme in anaerobic metabolism of Escherichia coli and other facultative anaerobes. PFL is a glycyl radical enzyme, which play key roles in anaerobic metabolism in microbes, including the reduction of ribonucleotides to deoxyribonucleotides, synthesis of benzylsuccinate, and conversion of choline to trimethylamine |
745316 |