Fundamentals of Biochemistry: Life at the Molecular Level 5th Edition

Published by Wiley
ISBN 10: 1118918401
ISBN 13: 978-1-11891-840-1

Chapter 11 - Enzymatic Catalysis - Exercises - Page 359: 26

Answer

The enzyme lysozyme degrades the bacterial cell wall. It hydrolyzes glycosidic bond from N-acetylmuramic (NAM) acid to N-acetylglucosamine (NAG). It converts acetal group into hemiacetal group. Glu 35 and Asp 52 are the catalytic residues of lysozymes. This enzymatic reaction should include an acid catalyst and a stabilization of transition state of oxonium ion (to convert from acetal to hemiacetal). Steps involves * General acid catalysis (oxonium ion formation) * Covalent catalysis * Covalent intermediate * Water binding and * Genereal base catalysis. Mutation of Glu 35 and Asp 52 to Glu is responsible for low catalytic activity of the enzyme and decreased binding property of the enzyme to substrates.

Work Step by Step

The enzyme lysozyme degrades the bacterial cell wall. It hydrolyzes glycosidic bond from N-acetylmuramic (NAM) acid to N-acetylglucosamine (NAG). It converts acetal group into hemiacetal group. Glu 35 and Asp 52 are the catalytic residues of lysozymes. This enzymatic reaction should include an acid catalyst and a stabilization of transition state of oxonium ion (to convert from acetal to hemiacetal). Steps involves * General acid catalysis (oxonium ion formation) * Covalent catalysis * Covalent intermediate * Water binding and * Genereal base catalysis. Mutation of Glu 35 and Asp 52 to Glu is responsible for low catalytic activity of the enzyme and decreased binding property of the enzyme to substrates.
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