Final answer:
The statement about pyruvate kinase being used in gluconeogenesis is false. Gluconeogenesis has its specific key enzymes which do not include pyruvate kinase, but instead include enzymes like PEPCK and glucose-6-phosphatase.
Step-by-step explanation:
The statement 'Pyruvate kinase is used in the process of gluconeogenesis' is false. In gluconeogenesis, which is the process of glucose synthesis from pyruvate or other molecules such as lactate, glycerol, or certain amino acids, pyruvate kinase is not utilized. Instead, key enzymes specific to gluconeogenesis are used to catalyze steps that are not simply the reverse of the glycolytic pathway.
These enzymes include pyruvate carboxylase, phosphoenolpyruvate carboxykinase (PEPCK), fructose-1,6-bisphosphatase, and glucose-6-phosphatase. Pyruvate kinase, on the other hand, functions in the last step of glycolysis, which is a different metabolic pathway where glucose is broken down into pyruvate and ATP is produced.
Pyruvate kinase is not involved in gluconeogenesis; instead, it plays a role in glycolysis. Gluconeogenesis is the process of synthesizing glucose from non-carbohydrate precursors, and it occurs mainly in the liver and kidneys. In gluconeogenesis, pyruvate is converted to glucose, and the reactions involved are distinct from those in glycolysis.
The conversion of pyruvate to phosphoenolpyruvate (PEP) in gluconeogenesis is catalyzed by the enzyme pyruvate carboxylase, not pyruvate kinase. Pyruvate kinase is part of glycolysis, where it catalyzes the conversion of phosphoenolpyruvate to pyruvate.