HW 2 - Academic Computing) or write out your response on...

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1) How are flavins and NADH similar? How are they different? 2) Tryptophan halogenase uses FAD as a cofactor. What other, inorganic cofactors are often found in halogenase enzymes? What do these cofactors have in common with flavins? (Hint: what is the oxidation state of Cl in the proposed mechanism?) 3) Cytochrome P450 enzymes catalyze the regio- and stereospecific incorporation of hydroxyl groups into organic substrates. They do so by utilizing a high-valent Fe(IV)=O species that allows formation of a –OH radical. Name a class of halogenase enzymes that follow a similar mechanism. How are these mechanisms similar/different? For the next two questions, you will need to either use a chemical drawing program (like Chemdraw, available for this course through
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Unformatted text preview: Academic Computing) or write out your response on paper and scan it. Please upload the answers as a separate file (button below). 4) Ornithine Decarboxylase is a PLP dependent enzyme that catalyzes the decarboxylation of ornithine to form putrescine in bacteria. Provide an arrow pushing mechanism to this decarboxylation event. 5) Malonyl CoA is a key subunit in polyketide and fatty acid biosyntheses. The biosynthesis of malonyl CoA begins with CoA-SH, pyruvate, ATP, and carbonate and utilizes the cofactors thiamin-pyrophosphate, lipoic acid, and biotin. Provide arrow pushing mechanisms to show this entire pathway....
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