Acid-base catalysis two part catalytic process (for example, the chymotrypsin mechanism) a covalent bond forms between enzyme and substrate Covalent catalysis Answer Bank may use amino acids such as aspartate or lysine for protonation or proton abstraction may take part in interactions involving Fe²+ Metal ion catalysis catalyst retains its original form after reaction occurs a proton is transferred between enzyme and substrate a Zn²+ cofactor orient the substra
Acid-base catalysis two part catalytic process (for example, the chymotrypsin mechanism) a covalent bond forms between enzyme and substrate Covalent catalysis Answer Bank may use amino acids such as aspartate or lysine for protonation or proton abstraction may take part in interactions involving Fe²+ Metal ion catalysis catalyst retains its original form after reaction occurs a proton is transferred between enzyme and substrate a Zn²+ cofactor orient the substra
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Transcribed Image Text:Enzymes use several types of catalytic mechanisms. Differentiate between acid-base catalysis, covalent catalysis, and metal
ion catalysis.
Acid-base catalysis
two part catalytic process (for example,
the chymotrypsin mechanism)
a covalent bond forms
between enzyme and substrate
lowers the energy or stabilizes
the transition state or intermediate
Covalent catalysis
Answer Bank
may use amino acids such as
aspartate or lysine for
protonation or proton abstraction
may take part in interactions
involving Fe²+
catalysts may participate in
oxidation-reduction reactions
by changes in the oxidation state
Metal ion catalysis
catalyst retains its original
form after reaction occurs
a proton is transferred
between enzyme and substrate
uses a nucleophilic
functional group
All
a Zn²+ cofactor may properly
orient the substrate in the active
site through ionic interactions
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