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Lecture

BIOCH 200 (February 28, 2014) - Enzymes

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Department
Biochemistry
Course
BIOCH200
Professor
Walter Dixon
Semester
Winter

Description
BIOCH 200: Enzymes (February 28, 2014) • *There are 2 ways of enhancing reaction rate: o *Adding heat  Not good for biological reactions since excess heat causes denaturation  Good for organic chemistry reactions though o *Adding a catalyst  Most common = enzymes  Other catalysts include certain metals (ex. platinum) • Enzymes are typically globular (there are exceptions) o *Globular protein shape lends more functional capabilities o Enzymes are a catalyst characteristic of biological systems o *Structure is determined by hydrophobic effects, H-bonding, ionic bonding (+/- charged amino acids interacting with each other), disulphide bridges (intramolecular and intermolecular) o Enzymes are also specific in their function  That being said: Enzyme function is completely determined by their conformation/shape • Enzymes vs. Non-biological catalysts o *Enzymes lend higher reaction rates, milder reaction conditions, greater reaction specificity (while heat can catalyze a lot of different reactions, enzymes will have a specific reaction that they affect) o Enzymes are more easily regulated and are important for cooperativity concerning ligand binding. • *ALMOST ALL ENZYMES ARE PROTEINS • Enzymes accelerate reaction rate AND are recovered at the end. o Increase rxn rate by 10 to 10 x0 • Nomenclature o *Typically end in “-ase”  Ex. catalase o *Typically contain substrate/product name and the chemical reaction.  Ex. citrate synthase  enzyme that synthesizes citrate  Ex. alcohol dehydrogenase  enzyme that removes hydrogen from alcohol molecules  Ex. pyruvate decarboxylase  enzyme that removes carboxyl groups from pyruvate • Enzymes are regulated. o Some of this regulation comes from changes in shape which could change or inactivate a function • *How do enzymes work? o *Work by decreasing the activation energy needed for a reaction to proceed.  *Stabilizes the transition state by reducing its free energy  *Activation energy is notated: ΔGǂ • Weird symbol is called: “double dagger” • *Activation energy = free energy of the transition state - free energy of the end product. o I-Clicker information:
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