Cysteine proteases are catalytically homologous to serine proteases, where the active site serine is replaced with a cysteine. What would be the appropriate order of the mechanism? Just write the numbers in order.
Cysteine proteases are catalytically homologous to serine proteases, where the active site serine is replaced with...
End Of Chapter, Problem 36 Get help answering Molecu Cysteine proteases include a catalytically active cysteine residue and can often be inactivated by iodoacetate (ICH2C00-). Show the product for the chemical reaction between the cysteine and iodoacetate. For your answer, follow these guidelines: 1. Draw the product with the correct ionization for pH 7.0. 2. Do not abbreviate any carboxylic acid groups; for example, do not use COOH. 3. Do not include hydrogens for carbon atoms. SH + C- Edit
1.. Example questions to guide you through the mechanism study of Serine proteases Describe substrate binding, including the role and chemical nature of the "specificity pocket" in chymotrypsin, and which peptide bond in the substrate (relative to the specificity group) will be cleaved. Draw the structure of the catalytic triad at the beginning of the reaction, and explain how the states of ionization and hydrogen bonding pattern of those 3 groups change step by step during catalysis. Explain the role...
Are the following examples of general acid/base catalysis, covalent catalysis, catalysis by approximation (proximity effect), or metal-ion catalysis? Complete parts a, b, c, and d. (b) NMP kinases bring two nucleotides, for example AMP and ATP, together to facilitate the transfer of a phosphoryl group from one nucleotide to the other (creating two ADP). The enzyme positions the adenosine triphosphate (ATP) such that the gamma phosphate group is placed adjacently to the phosphate group of the NMP kinase. This facilitates...
Under typical conditions, many essential biochemical reactions proceed so slowly that life could not exist without the presence of enzymes. Enzymes increase reaction rates through a wide variety of mechanisms. These mechanisms generally utilize the following strategies: improving the nucleophiles and electrophiles present in the catalytic R groups or substrates; stabilizing the extra electron density of the leaving group; and stabilizing transition states. Proteases are enzymes that break down proteins by hydrolyzing peptide bonds. Chymotrypsin is a protease found in...
The active site of an enzyme ____. A. is remote form the site of substrate attachment B. is converted to a product C. is the region where the reaction takes place D. increases the energy of reaction E. includes the entire enzyme In the lock-and-key model of enzyme actin, the enzyme active site is thought of as ___. A. a rigid, nonflexible shape that fits the substrate exactly B. an area of the enzyme that can adjust to fit the...