Answer: This question is incomplete. Here is the complete question:
The ATP that is generated in glycolysis is produced by substrate-level phosphorylation, a very different mechanism than the one used to produce ATP during oxidative phosphorylation. Phosphorylation reactions involve the addition of a phosphate group to another molecule.
Sort the statements into the appropriate bin depending on whether or not they correctly describe some aspect of substrate-level phosphorylation in glycolysis.
-One of the substrates is a molecule derived from the breakdown of glucose
-An enzyme is required in order for the reaction to occur
-A bond must be broken between an organic molecule and phosphate before ATP can form.
-The phosphate group added to ADP to make ATP comes from free inorganic phosphate ions.
-The enyzmes involved in ATP synthesis must be attached to a membrane to produce ATP.
The correct statements are , Statements 1,2&3.
The incorrect statements are 4&5.
Explanation: Statement 1 is correct because the two substrates involved in substrate-level phosphorylation in glycolysis are 1,3-bisphosphoglycerate and phosphoenolpyruvate which are both derived from the breakdown of glucose.
Statement 2 is correct because enzymes are required in both of the reactions. The enzymes are phosphoglycerate kinase and pyruvate kinase.
Statement 3 is correct because the bond between the substrates (organic molecules) and the phosphate groups must be be broken first before the phosphate groups are linked to ADP to form ATP.
Statement 4 is incorrect because the phosphate added to ADP to form ATP are not free inorganic phosphates but are bound to the substrates, 1,3-bisphosphoglycerate and phosphoenolpyruvate.
Statement 5 is incorrect because substrate-level phosphorylation involve soluble enzymes. Both phosphoglycerate kinase and pyruvate kinase are soluble and not membrane-bound enzymes found in the cytosol of glycolytic cells.
