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Proteins (tertiary and quaternary structures) Act as Catalyst to accelerate a reaction Not permanently changed in the process
Enzymes
Are specific
Destaining fabrics
Dehairing hides Recovering silver from photographic films Wound healing Augmentingsurgery Disolving Blood clot ClinicaL Chemistry Bioremediation Bioprocessing
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Biofermentor
Production f Chemicals
Enzymes
Without Enzyme With Enzyme
Free Energy
Products
Enzyme
Active Site
A restricted region of an enzyme
Enzyme
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Induced Fit
A change in the
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Induced Fit
A change in the configuration of an
enzymes active site (H+ and ionic bonds are involved). Induced by the substrate.
Active Site substrate Enzyme induced fit
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1. Environmental Conditions
1. Extreme Temperature are the most dangerous - high temps may denature (unfold) the enzyme. 2. pH (most like 6 - 8 pH near neutral) 3. Ionic concentration (salt ions)
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Example: Iron must be present in the quaternary structure - hemoglobin in order for it to pick up oxygen.
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chemicals that resemble an enzymes normal substrate and compete with it for the active site.
Substrate
Competitive inhibitor
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Enzyme
Inhibitors
b. Noncompetitive inhibitors: Inhibitors that do not enter the active site, but bind to another part of the enzyme causing the enzyme to change its shape, which in turn alters the active site.
Substrate active site altered
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Enzyme
Noncompetitive Inhibitor
Regulation of Enzymes
Regulation of enzymatic
pathways prevent the deletion of substrate Regulation happens at the level of the enzyme in a pathway Feedback inhibition is when the end product regulates the enzyme early in the pathway
Feedback Regulation
Negative feedback
pathway is inhibited by accumulation of final product Positive feedback a regulatory molecule stimulates the activity of the enzyme, usually between 2 pathways
ADP levels cause the
Allostery
Conformational coupling of 2 widely
separated binding sites must be responsible for regulation active site recognizes substrate and 2nd site recognizes the regulatory molecule Protein regulated this way undergoes allosteric transition or a conformational change Protein regulated in this manner is an allosteric protein
Allosteric Regulation
Allosteric Regulation
Phosphorylation
Some proteins are regulated by the addition of a
PO4 group that allows for the attraction of + charged side chains causing a conformation change Reversible protein phosphorylations regulate many eukaryotic cell functions turning things on and off Protein kinases add the PO4 and protein phosphatase remove them
Phosphorylation/Dephosphorylation
Kinases capable of
group
Serine Threonine
Tyrosine
Phosphatases that