Note: Given data indicated as alphabet and actual data in numericals
A--->1
B--->2
G--->3
C--->4
E--->5
F--->6
D--->7
H--->8
Put these steps in the mechanism of chymotrypsin catalysis in order from first to last. Note...
Put these steps in the mechanism of chymotrypsin catalysis in order from first to last. Note that your textbook may not break out each of these steps individually, but all steps should be ordered. (There will be eight steps. ) first step last step Resulting OH attacks carbonyl of remaining substrate. His 57 donates H to Ser 195 O, leading to collapse of tetrahedral intermediate. mato Ser 195 the portion (N-terminal end) of original substrate with the new carboxylate terminus...
Put these steps in the mechanism of chymotrypsin catalysis in order from first to last. Note that your textbook may not break out each of these steps individually, but all steps should be ordered. (There will be eight steps.) A. His 57 catalyzes removal of H from Ser 195 hydroxyl. B. His 57 donates H to N of sissile peptide bond, tetrahedral intermediate decomposes. C. The portion (N-terminal end) of the original substrate with the new carboxylate terminus diffuses away....
Chymotrypsin What evidence in chymotrypsin mechanism supports the claim that chymotrypsin catalysis involves general acid-base catalysis and covalent catalysis? Draw the chemical structure of the transition state (resembles the intermediate structure) in the step that forms the enzyme-product covalent adduct. In comparison to the substrate, how is the tetrahedral transition state preferentially stabilized by enzyme? Chymotrypsin mechanism: Write all the steps in the mechanism and understand what each step accomplishes.