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Phosphorylation of glucose is a key reaction in sugar metabolism. The chemical equation for the conversion of D-glucose to D-glucose-6-phosphate in the first step of glycolysis is given by: D-glucose + ATP → D-glucose 6-phosphate + ADP ΔG° = −16.7 kJ/mol (° indicates measurement at standard condition)
d -Glucose + 2 [NAD] + + 2 [ADP] + 2 [P] i 2 × Pyruvate 2 × + 2 [NADH] + 2 H + + 2 [ATP] + 2 H 2 O Glycolysis pathway overview The use of symbols in this equation makes it appear unbalanced with respect to oxygen atoms, hydrogen atoms, and charges. Atom balance is maintained by the two phosphate (P i) groups: Each exists in the form of a hydrogen phosphate anion, dissociating to contribute ...
The anaerobic glycolysis (lactic acid) system is dominant from about 10–30 seconds during a maximal effort. It produces 2 ATP molecules per glucose molecule, [3] or about 5% of glucose's energy potential (38 ATP molecules). [4] [5] The speed at which ATP is produced is about 100 times that of oxidative phosphorylation. [1]
Glucose-6-phosphate can then progress through glycolysis. [1] Glycolysis only requires the input of one molecule of ATP when the glucose originates in glycogen. [1] Alternatively, glucose-6-phosphate can be converted back into glucose in the liver and the kidneys, allowing it to raise blood glucose levels if necessary. [2]
The cleaved molecule is in the form of glucose 1-phosphate, which can be converted into G6P by phosphoglucomutase. Next, the phosphoryl group on G6P can be cleaved by glucose 6-phosphatase so that a free glucose can be formed. This free glucose can pass through membranes and can enter the bloodstream to travel to other places in the body.
Physiologically normal intracellular pH is most commonly between 7.0 and 7.4, though there is variability between tissues (e.g., mammalian skeletal muscle tends to have a pH i of 6.8–7.1). [4] [5] There is also pH variation across different organelles, which can span from around 4.5 to 8.0. [6] [7] pH i can be measured in a number of ...
Glucose-6-phosphate dehydrogenase is the rate-controlling enzyme of this pathway [citation needed]. It is allosterically stimulated by NADP + and strongly inhibited by NADPH. [7] The ratio of NADPH:NADP + is the primary mode of regulation for the enzyme and is normally about 100:1 in liver cytosol [citation needed]. This makes the cytosol a ...
An acid-base diagram for human plasma, showing the effects on the plasma pH when P CO 2 in mmHg or Standard Base Excess (SBE) occur in excess or are deficient in the plasma [23] Acid–base imbalance occurs when a significant insult causes the blood pH to shift out of the normal range (7.32 to 7.42 [ 16 ] ).