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Biochemistry Ch. 2 - Enzymes
MCAT
22
Biochemistry
Undergraduate 3
03/23/2016

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Term
ribozymes
Definition
biological catalysts composed of RNA instead of peptides
Term
What are the six major groups of enzymes?
Definition
- lyases
- isomerases
- ligases
- hydrolases
- oxidoreductases
- transferases
Term
oxidoreductases
Definition
catalyze redox reactions; common cofactors are NAD+ and heme
Term
transferases
Definition
move a functional group from one molecule to another; named as trans[functional group]ase or [functional group] transferase
Term
hydrolases
Definition
catalyze cleavage without the addition of water; phosphatase, peptidases, nucleases, lipases
Term
lyase
Definition
catalyze cleavage without the addition of water and without the transfer of electrons. The reverse reaction (synthesis) is often more important biologically; synthases
Term
isomerases
Definition
catalyze the interconversion of isomers, including both constitutional isomers and stereoisomers; some can also be classified as other enzyme types depending on mechanism
Term
ligases
Definition
responsible for joining two large biomolecules, often of the same type
Term
lock and key theory
Definition
hypothesizes that the enzyme and substrate are exactly complementary
Term
induced fit model
Definition
hypothesizes that the enzyme and substrate under undergo conformational changes to interact fully
Term
coenzymes vs cofactors
Definition
  • small organic groups, mostly vitamins or vitamin derivatives (NAD, FAD, coenzyme A)
  • generally inorganic molecules or metal ions
Term
apoenzyme
Definition
enzyme without cofactor
Term
enzyme with cofactor
Definition
Term
Michaelis-Menten equation
Definition

v = (vmax[S])/(Km + [S])

Km = 1/2vmax

Km is the Michaelis Constant

[S] is substrate concentration

vmax is the maximal reaction velocity

 

Term
How to interpret Km
Definition
Km is a measure of substrate enzyme affinity, a higher Km equals a lower affinity
Term
Reading Lineweaver-Burke Plots
Definition
  • x-intercept equals -1/Km
  • y-intercept is the vmax
Term
What is the optimal pH of the blood, stomach and small intestine? Why does it matter?
Definition
7.4, 2 and 8.5; it is important for the function of the enzymes in that part of the body
Term
What are the four types of reversible inhibition?
Definition
  • competitive
  • noncompetitive
  • mixed
  • uncompetitive
Term

[image]

What kind of inhibition is this?

Definition
competitive inhibition, vmax stays the same, Km increases (meaning enzyme-substrate affinity decreases); this type can be overcome by adding more substrate; inhibitor binds the active site
Term

[image]

What kind of inhibition is this?

Definition
noncompetitive inhibition - decreases Vmax, Km stays same, binds to allosteric site inducing change in enzyme conformation
Term

[image]

what kind of inhibition is this?

Definition
uncompetitive inhibition - bind only to enzyme-substrate complex locking them together and preventing their release; lowers Km and vmax
Term

[image]

What kind of inhibition is this?

Definition
mixed inhibition - binds allosteric site and preferentially binds enzyme (increases Km) or enzyme substrate complex (decreases Km); vmax decreases in both cases
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