Exam 9: Catalytic Strategies
Exam 1: Biochemistry: An Evolving Science50 Questions
Exam 2: Protein Composition and Structure48 Questions
Exam 3: Exploring Proteins and Proteomes50 Questions
Exam 4: DNA, RNA, and the Flow of Genetic Information41 Questions
Exam 5: Exploring Genes and Genomes50 Questions
Exam 6: Exploring Evolution and Bioinformatics47 Questions
Exam 7: Hemoglobin: a Portrait of a Protein in Action53 Questions
Exam 8: Enzymes: Basic Concepts and Kinetics50 Questions
Exam 9: Catalytic Strategies50 Questions
Exam 10: Regulatory Strategies50 Questions
Exam 11: Carbohydrates49 Questions
Exam 12: Lipids and Cell Membranes50 Questions
Exam 13: Membrane Channels and Pumps52 Questions
Exam 14: Signal-Transduction Pathways50 Questions
Exam 15: Metabolism: Basic Concepts and Design50 Questions
Exam 16: Glycolysis and Gluconeogenesis50 Questions
Exam 17: The Citric Acid Cycle48 Questions
Exam 18: Oxidative Phosphorylation50 Questions
Exam 19: The Light Reactions of Photosynthesis50 Questions
Exam 20: The Calvin Cycle and the Pentose Phosphate Pathway48 Questions
Exam 21: Glycogen Metabolism50 Questions
Exam 22: Fatty Acid Metabolism50 Questions
Exam 23: Protein Turnover and Amino Acid Catabolism49 Questions
Exam 24: The Biosynthesis of Amino Acids48 Questions
Exam 25: Nucleotide Biosynthesis50 Questions
Exam 26: Biosynthesis of Membrane Lipids and Steroids50 Questions
Exam 27: The Integration of Metabolism50 Questions
Exam 28: DNA Replication, repair, and Recombination48 Questions
Exam 29: RNA Synthesis and Processing47 Questions
Exam 30: Protein Synthesis48 Questions
Exam 31: The Control of Gene Expression in Prokaryotes49 Questions
Exam 32: The Control of Gene Expression in Eukaryotes50 Questions
Exam 33: Sensory Systems49 Questions
Exam 34: The Immune System50 Questions
Exam 35: Molecular Motors50 Questions
Exam 36: Drug Development48 Questions
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What type of assay allows analysis of an enzyme catalyzed reaction in milliseconds?
(Multiple Choice)
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Which of the following techniques allows investigators to test the role of individual amino acids in the determination of enzyme structure/function relationships even if the investigated amino acid is not present in the active site?
(Multiple Choice)
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What caused a "burst" of activity followed by a steady-state reaction when chymotrypsin was studied by stop-flow techniques?
(Essay)
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In chymotrypsin,the tetrahedral intermediate transition state is stabilized by a structural feature referred to as the "___________________" hole.
(Short Answer)
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If you carried out site-directed mutagenesis of subtilisin,changing serine 221 to isoleucine,what would you expect?
(Multiple Choice)
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Complete the structure of the catalytic triad of chymotrypsin by drawing the proper structure of the missing residue side chain in the box provided.Show the proper hydrogen bonding involved in this triad. 
(Essay)
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Which of the following is an enzyme that temporarily undergoes covalent catalysis as part of its mechanism?
(Multiple Choice)
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A-T base pairs,which contain _____ hydrogen bonds,are more easily interrupted than G-C base pairs with _______ hydrogen bonds.
(Short Answer)
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What metal ion is frequently found in enzyme active sites that act on phosphate-containing substrates?
(Multiple Choice)
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Describe the secondary and tertiary structures in domains that form P-loops and bind phosphoryl groups.
(Essay)
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How can covalent modification be used to determine the mechanism of action of an enzyme?
(Essay)
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What mechanism is responsible for restriction endonuclease cleavage of DNA?
(Essay)
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What is the common strategy for cysteine,metallo-,and aspartyl proteases?
(Essay)
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What metal ion is required by carbonic anhydrase for activity?
(Multiple Choice)
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Which amino acids in chymotrypsin are found in the active site and are participants in substrate cleavage?
(Multiple Choice)
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