Unformatted text preview: amino group is 10.5. A novel enzyme, tyrosine aminomutase, which catalyses the conversion of L‐α‐tyrosine to β‐
tyrosine, was isolated from Streptomyces globisporus. To investigate the kinetics of the novel enzyme, the initial rate of reaction was measured with variable initial concentrations of L‐α‐
tyrosine, in the absence and presence of inhibitor H. The following data was obtained: [L‐α‐Tyrosine] Initial Rate (µM/sec) (mM) Without Inhibitor H With Inhibitor H 0.0125 0.0250 0.0500 0.0750 0.1000 0.2000 0.2500 1.0000 (a) (b) (c) (d) (e) 5. 0.0295 0.0465 0.0670 – 0.0835 – 0.1045 0.1105 – – 0.0145 0.0210 0.0260 0.0435 – 0.0790 Which Enzyme Commission class should this enzyme be classified under? Provide both the class number and name. Using the Lineweaver‐Burk double‐reciprocal plot, determine the Km (in µM) and Vmax (in µM/sec) values of the novel tyrosine aminomutase. On the same graph, determine the apparent Km and Vmax values (in µM and µM/sec, respec...
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- Spring '12
- Biochemistry, Aspartic acid, Vmax values, Inhibitor Inhibitor, inhibitor H.