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HW 3 - complexes and how are they similar to fungal FAS 4...

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1) How do the architectures of fungal FAS and mammalian FAS differ? How are these FAS enzymes different from those in bacteria and plants? 2) In the study by Leibundgut et al., the ACP is stalled at the KS domain. Looking at the active site of KS and the end of the ACP prosthetic group, what kind of covalent linkage could be responsible for trapping the ACP? 3) In this study, the authors report evidence that FAS is evolutionarily related to other enzyme complexes containing carrier proteins bearing a prosthetic group? What are these enzyme
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Unformatted text preview: complexes and how are they similar to fungal FAS? 4) How many times does the ACP domain interact with/bind the Ketosynthase domain in each extension cycle (ie. each time the chain gets extended by 2 carbons)? What is the oxidation state of the carbon β to the thioester in each case (ie. methylene, α/β unsaturated, β-hydroxy, β-keto, carboxylate, etc.)? 5) There are two steps in the catalytic mechanism of thioesterase domains. What are these two steps? Which one involves association with ACP? Which one is rate-limiting?...
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