2A. Red blood cells synthesize and degrade 2,3-bisphosphoglycerate (2,3-BPG) by a detour of theglycolytic pathway, as shown below:glyeeraldehyde 3-phosphateGAP dehydrogenase1,3-bisphosphoglyceratebisphosphoglycerate mutaseADPphosphoglycerate kinase2,3-bisphosphoglycerateATP3-phosphoglycerate2,3-bisphosphoglycerate phosphatasephosphoglycerate mutase2-phosphoglycerate(i) The bisphosphoglycerate mutase/2,3-bisphosphoglcerate phosphatase reaction is catalyzed by a single enzyme,BPGM. At alkaline pH, BPGM favors the mutase activity while at lower pH, BPGM favors the phosphatasereaction. Use this information, along with the Bohr effect, to explain in the space below how red blood cellsrespond to a metabolic defect where a patient experiences chronic, elevated levels of lactic acid. I(ii) Individuals with red blood cell phosphoglycerate kinase deficiency suffer from moderate hemolytic anemia (acondition where red blood cells self-destruct before their normal lifespan). They also have unusual levels of ATPand 2,3-BPG. Predict what is unusual about the ATP and 2,3-BPG levels in this genetic disorder and explain whythese patients suffer from mild hemolytic anemia

1) At alkaline pH BPGM show the mutase activity. Here the enzyme Bisphosphoglycerate mutase (BPGM) is a unique type of enzyme found in erthrocytes and placental cells. Its function is to synthesize 2,3-BPG. The 2,3-BPG can change the equilibrium of hemoglobin toward the deoxy-state and binds with the high affinity conformational change that release the oxygen. While at hemoglobin which cause a lower pH BPGM favors the phosphatase reaction. 2,3-bisphosphoglycerate phosphatase is a enzyme that can undergo degradation and synthesis of 2,3-BPG. During chronic condition increase in the body is known as Lactic acidosis. In lactic acidosis is a condition which body start to buildup lactate, which low the pH of blood. According to Bohr effect, which state that any change in pH lead to effect the binding affinity of oxygen to hemoglobin. In the above of Lactic acidosis were pH of blood is low. Under lower pH condition (high H+) the side chain of histidine (which bind to the oxygen molecule) deoxyhemoglobin become stable were lactic level becomes protonated and deoxyhemoglobin become stable. 2) Hemolytic anemia is a type of anemia which is cause due to hemolysis. Hemolysis means abnormal breakage of the RBCs and other blood vessels. Intrinsic type of hemolytic anemia defect cause of RBCS production and metabolism which lass generation to generation (hereditary). During mild Hemolytic anemia, it modify the RBCs life cycle(normally 90 to 120 days lifespan of RBCs). That's, rather than being collected at the conclusion of its valuable life and aranged of regular, the RBC crumbles ina way permitting free iron-containing atoms to reach the blood. With lack of mitochondria, RBCs depend on gylcolysis for the ATP or energy to reduce the oxidative harm. Any blockage of glycolysis leads to oxidative damage and irregular lifespan of RBCs. So if ATP production is uneven, it will effect the production of 2,3-BPG. 2,3-BPG direct relate to the pH of the blood and oxygen binding affinity to hemoglobin.