Chapter 9 - Mechanisms Flashcards
What are the 4 catalytic principles?
covalent catalysis
acid base catalysis
catalysis by approximation
metal ion catalysis
what is covalent catalysis?
an enzyme makes a covalent bond by itself
the covalent bond will need to break to not use up all the energy in for the enzyme to continue its reaction
what is acid base catalysis?
enzyme is acting as an acid or base or both in the process of catalysis
not an acid base reaction but the enzyme is an acid by donating a proton and accepts a proton and is a base
what is catalysis by approximation?
the distance and the orientation is very specific
what is metal ion catalysis?
enzymes use metal ion as prosthetics
How many catalytic principles do enzymes usually follow>
they use at least one but most use more than one
proteases hydrolyze what bond?
the peptide bond
how are protease families divided?
They are divided by what they do
which enzymatic principle is involved in all enzymes?
catalysis by approximation
what is the other substrate involved in a proteases hydrolysis?
the peptide bond (is the implied one)
water
what are the products for a proteases hydrolosis?
carbonyl containing product
amine containing product
how do we classify enzymes?
by what they do
what group is a protease? And what does that class do?
proteases are a class of enzymes
cut peptide bonds
if you hydrolyze a peptide bond what are you?
a protease
what does the term family mean?
they have a common ancestor (similar by genealogical evolutionary relation)
what makes you a member of a family?
where you come from
what makes you a protease?
cut peptide bonds
or what you do
in order to be a member of the class of proteases you need to be able to do what?
hydrolyze a peptide bond
what are some of the families of proteases?
serine
how is the serine protease family “related”?
because they are inhibited by certain irreversible competitive inhibitors.
have homologous tertiary structures (because of having homologous primary structure)
Because the serine protease family has homology in tertiary structure what is that due to?
having homology in there primary structure
What makes a serine protease part of this family?
they have varying substrate specificity but use the same catalytic mechanism
What are two examples of a serine protease?
Chymotrypsin and Trypsin
they are digestive enzymes in your gut
how is chymotrypsin and trypsin similar and how are they different?
similar:
- active site
- they use the same mechanisms
- use covalent catalysis
differences:
- trypsin has an aspartic acid in the active site
- chymotrypsin cuts after an aromatic amino acid (Phenylalanine, tryptophan, tyrosine)
- trypsin with its negative charge cuts after the basic amino acids (lysine or arginine, (positively charged))