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ERIC Number: EJ948597
Record Type: Journal
Publication Date: 2011
Pages: 3
Abstractor: As Provided
Reference Count: 5
ISSN: ISSN-1470-8175
An Easy and Effective Demonstration of Enzyme Stereospecificity and Equilibrium Thermodynamics
Herdman, Chelsea; Dickman, Michael
Biochemistry and Molecular Biology Education, v39 n5 p341-343 Sep-Oct 2011
Enzyme stereospecificity and equilibrium thermodynamics can be demonstrated using the coupling of two amino acid derivatives by Thermoase C160. This protease will catalyze peptide bond formation between Z-L-AspOH and L-PheOMe to form the Aspartame precursor Z-L-Asp-L-PheOMe. Reaction completion manifests itself by precipitation of the product. As the product has almost zero solubility, the equilibrium favors condensation and thus a normally hydrolytic enzyme catalyzes the opposite reaction. Neither Z-D-AspOH with L-PheOMe nor Z-L-AspOH with D-PheOMe produces any visible product. (Contains 3 figures and 1 table.)
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Publication Type: Journal Articles; Reports - Descriptive
Education Level: Higher Education
Audience: N/A
Language: English
Sponsor: N/A
Authoring Institution: N/A