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Glycolysis is the metabolic pathway that converts glucose (C 6 H 12 O 6) into pyruvate and, in most organisms, occurs in the liquid part of cells (the cytosol). The free energy released in this process is used to form the high-energy molecules adenosine triphosphate (ATP) and reduced nicotinamide adenine dinucleotide (NADH). [1]
"The metabolic pathway of glycolysis converts glucose to pyruvate via a series of intermediate metabolites. Each chemical modification (red box) is performed by a different enzyme. Steps 1 and 3 consume ATP (blue) and steps 7 and 10 produce ATP (yellow). Since steps 6-10 occur twice per glucose molecule, this leads to a net production of energy."
Glycolysis enzymes (10 P) Pages in category "Glycolysis" The following 39 pages are in this category, out of 39 total. This list may not reflect recent changes. ...
Pages in category "Glycolysis enzymes" The following 10 pages are in this category, out of 10 total. This list may not reflect recent changes. E. Enolase; F.
Glucose regulation and product use are the primary categories in which these pathways differ between organisms. [2] In some tissues and organisms, glycolysis is the sole method of energy production. [2] This pathway is common to both anaerobic and aerobic respiration. [1] Glycolysis consists of ten steps, split into two phases. [2]
Anaerobic glycolysis is thought to have been the primary means of energy production in earlier organisms before oxygen was at high concentration in the atmosphere and thus would represent a more ancient form of energy production in cells. In mammals, lactate can be transformed by the liver back into glucose using the Cori cycle.
PGK is a major enzyme used in glycolysis, in the first ATP-generating step of the glycolytic pathway. In gluconeogenesis, the reaction catalyzed by PGK proceeds in the opposite direction, generating ADP and 1,3-BPG. In humans, two isozymes of PGK have been so far identified, PGK1 and PGK2.
The systematic name of this enzyme is 2-phospho-D-glycerate hydro-lyase (phosphoenolpyruvate-forming). The reaction is reversible, depending on environmental concentrations of substrates. [3] The optimum pH for the human enzyme is 6.5. [4] Enolase is present in all tissues and organisms capable of glycolysis or fermentation.