Esterase hydrolyzes ester bonds. For simplicity, only the amino acids whose side-chains interact with the substrate are shown. Each circled interaction is important for the binding of the substrate to the enzyme. substrate x LCH- CH, CH Z CH, H,C CH, H3C. Esterase active site

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Chapter21: Biochemistry
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Problem 28QAP: . Describe the lock-and-key model for enzymes. Why are the shapes of the enzyme and its substrate...
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Esterase hydrolyzes ester bonds. For simplicity, only the amino acids whose side-chains
interact with the substrate are shown. Each circled interaction is important for the binding
of the substrate to the enzyme.
substrate
x CH,-O
CH Z
H3C
CH, H,C
CH,
Esterase
active site
Full activity of esterase is observed at 37°C and a pH of 7.4. You isolate the active form of
esterase, subject it to a high salt (high sodium chloride) concentration and show that it cannot bind
the substrate. You then return the sample to the original conditions and measure the substrate
binding ability of the esterase again.
Would the esterase bind to its substrate when returned to the pretreatment conditions
(Yes/No)? Explain.
Transcribed Image Text:Esterase hydrolyzes ester bonds. For simplicity, only the amino acids whose side-chains interact with the substrate are shown. Each circled interaction is important for the binding of the substrate to the enzyme. substrate x CH,-O CH Z H3C CH, H,C CH, Esterase active site Full activity of esterase is observed at 37°C and a pH of 7.4. You isolate the active form of esterase, subject it to a high salt (high sodium chloride) concentration and show that it cannot bind the substrate. You then return the sample to the original conditions and measure the substrate binding ability of the esterase again. Would the esterase bind to its substrate when returned to the pretreatment conditions (Yes/No)? Explain.
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