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Lecture

Enzymes and Glycolysis

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Department
Biology (Sci)
Course
BIOL 112
Professor
Frieder Schoeck
Semester
Winter

Description
← Lecture 10 ← Enzymes and Glycolysis ← Friday February 8 2013 ← ← Catalyst: any substance that speeds up a chemical reaction without itself being used up • Only reactions with overall –ΔG can be catalyzed • Biological systems can’t initiate reactions by adding heat therefore enzymes are used to lower the activation energy ← ← Enzymes • bind to the active site on specific substrates where they catalyze • catalyze reactions by using 1+ of: o Orienting substrates o Inducing strain in the substrates o Adding charges to substrates • Cofactors: metal ions/small organic molecules that are temp or permanently bound to the enzyme – required for some enzymes • Enzymes (E’s) get saturated when all binding sites are occupied • Metabolic Pathways o Feedback inhibition end-product regulates the whole pathway o Each reaction in the path is catalyzed by a specific enzyme • Enzyme Regulation o E activity can be inhibited by natural and artificial binders, some are irreversible b/c they destroy the enzyme o Competitive inhibitor: binds reversibly to an E’s active site o Noncompetitive inhibitor/negative allosteric regulator: changes the shape of the E by binding reversibly to somewhere other than the active site, ends up changing the active site so it can’t bind with the substrate o Allosteric regulators: can stabilize the active form (+ allosteric regulator) or stabilize the inactive form (- A. R) of the E  Much more efficient than competitive inhibition  Cooperative allosteric transition: occurs with 2+ subunits  When 1 binding site is occupied, it changes the others so that they bind other substrates more readily  E activation or inhibition occurs very quickly  First step in a metabolic pathway almost always a multi-subunit E negatively regulated by cooperative allostery Glycolysis and Redox Reactions • Glycolysis is followed by 2 metabolic processes o 1. Cellular
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