Cheat Sheet - Final Biochem Part VI

Capitulo 6/7 1- A structure of a common monosaccharide is shown. 2- Name the monosaccharides in the images by placing the appropriate terms. 3- Analyze the following pair of compounds. Which of the terms explains the relationship between the two compounds. 4- Put these steps in the mechanism of chymotrypsin catalysis in order from first to last. Note that some references may not break out each of these steps individually, but all steps should be ordered. There will be eight steps. 5- What is the catalytic triad of chymotrypsin, a type of serine protease? 6- Classify each phrase as describing a competitive inhibitor, uncompetitive inhibitor, or mixed (mixed noncompetitive) inhibitor. Note that 𝐾  m refers to apparent 𝐾   m . 7- Classify the phrases. Does each phrase describe a kinase, a phosphatase, neither, or both? 8- Analyze the following Double-Reciprocal plots and identify the correct statement represented by the diagram. 9- The graph shows three plots of velocity ( 𝑣0) versus substrate concentration ([S])  . Determine which curve represents an enzyme's reaction velocity without any inhibitor present, which curve represents the velocity in the presence of a mixed inhibitor, and which curve represents the velocity in the presence of a competitive inhibitor. 10- Analyze the pair of compounds. 11- Identify each glucose derivative by selecting the correct structure. 12- The following statements are all true with respect to proteolytic cleavage activation. 13- What are characteristics of allosteric enzymes? 14- Disaccharides are joined by glycosidic bonds formed between the anomeric carbon on one monosaccharide and a hydroxyl (−OH)   group of another monosaccharide. 15- Convert the Haworth projection for a monosaccharide to its corresponding Fischer projection. 16- Which of the following secuences is correct for the extrinsic pathway in Coagulation 17- Which of the following aminoacids is not utilized by Kinases? 18- Consider the image. Identify the structural name for the disaccharide in the image. 19- Consider the hypothetical serine protease in the image, which shows the specificity pockets. The S  1 pocket has a glutamic acid in the bottom, the S  2 pocket is small and hydrophobic, and the S  1 ′ pocket is deep and hydrophobic. Suggest a 3-amino acid sequence that this protease would cleave and indicate between which sites the peptide bond would be broken. 20- Classify the sugars based on whether they show mutarotation or not. 21- The Lineweaver–Burk plot, which illustrates the reciprocal of the reaction rate (1/  𝑣 ) versus the reciprocal of the substrate concentration (1/[S])   , is a graphical representation of enzyme kinetics. This plot is typically used to determine the maximum rate, 𝑉   max , and the Michaelis constant, 𝐾m , which can be gleaned from the intercepts and slope. Identify each intercept and the slope in terms of the constants  𝑉m   m .  ax and 𝐾 22- The Characteristic pH profile for Chymotripsin shown below, can be explained by: 23- An enzyme catalyzes the reaction M↽  −−⇀N . 24- What kind of inhibitors are transition state analogs usually classified as? 25- Select the graph that correctly illustrates the effect of a negative modifier (effector) on the velocity curve of an allosteric enzyme. Place the correct graph in the set of axes. The solid blue curve represents the unmodified enzyme. The dashed green curve represents the enzyme in the presence of the effector.