Biochemistry
Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 24, Problem 4P
Interpretation Introduction

Interpretation:

A maximal separation between the malonyl transferase and the β-ketoacyl-ACP synthase active sites should be estimated.

Concept Introduction:

Fatty acid synthase is a multi-enzyme protein which catalyzes the fatty acid biosynthesis.Major function is catalyzing the formation of palmitate from acetyl CoA and malonyl CoA. Mammalian fatty acid synthase contains two identical protein subunits. Three catalytic domains are in N-terminal section which are β-ketoacyl-ACP synthase, malonyl/acetyl transferase and dehydrase. Four catalytic domains are in C-terminal section, which are enoyl reductase, ketoacyl reductase, acyl carrier protein and thioesterase. N terminal section and C terminal section is separated by 600 residues.

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M-CSA Mechanism and Catalytic Site Atlas (ebi.ac.uk) (ii) Acyl Carrier Protein S-acetyltransferase (EC 2.3.1.38) is a transferase enzyme that catalyzes the first biosynthetic pathway for fatty acid synthase. It transfers the acyl group (CH3CO) first from coenzyme A to a cysteine residue in the active site. This is similar to what happens in Chymotrypsin, however utilizing a sulfur instead of an oxygen. The acyl group is then transferred to the molecule ACP. Provide the enzyme- catalyzed mechanism for the reaction below, making sure to identify the roles of all key amino acids: i H3C SCOA acetyl COA enzyme + HS i H3C SACP acetyl ACP
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