Biochemistry Exam 3

Biochemistry Exam 3 - Dr. Smith CH320 November 19, 2001...

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Unformatted text preview: Dr. Smith CH320 November 19, 2001 Biochemistry Exam 3 1) See the reactions below. a) Given the general mechanism for the hydrolysis of an alkene, design the active site for the enzyme which would catalyze the hydrolysis of fumarate to L- malonate. Be sure to show where residues should be placed in the active site and explain their role in the catalysis by drawing an abbreviated mechanism. b) Name the enzyme based on common naming conventions for enzymes. COO COO H H H 2 O COO COO H HO H OH 2 H H + OH 2 H HO H OH 2 HO H Fumarate L-malonate Hydrolysis of an Alkene Dr. Smith CH320 November 19, 2001 c) Use the following Lineweaver-Burk plot for the enzyme which catalyzes this reaction to determine its V max , K m , k cat and catalytic efficiency when [E] = 2 10-6 M. (Units for [S] are mM and for v are mM/mL*min.) Dr. Smith CH320 November 19, 2001 2) Which of the reactions below has a larger rate constant? Why? How does this relate to their Which of the reactions below has a larger rate constant?...
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This note was uploaded on 06/11/2008 for the course BI 350 taught by Professor Stedman during the Spring '08 term at Portland State.

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Biochemistry Exam 3 - Dr. Smith CH320 November 19, 2001...

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