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Enzymes are biological catalysts made of proteins that speed up chemical reactions in living organisms without being consumed in the process. They work by lowering the activation energy needed for a reaction to occur. Each enzyme has a specific active site that binds to its substrate with high specificity, often described by the "lock and key" or "induced fit" models. Enzymes follow Michaelis-Menten kinetics, characterized by parameters like Vmax (maximum reaction rate) and Km (substrate concentration at half Vmax). They can be regulated through inhibition (competitive, noncompetitive, uncompetitive), allosteric modulation, and covalent modifications (like phosphorylation). Environmental factors such as temperature, pH, and substrate concentration affect enzyme activity. Enzymes play essential roles in metabolism, signal transduction, DNA replication, and many other biological processes.
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-00C (^) NH? Globular Proteins
-00C →^ No^ binding
study of^ enzymatic processes → and (^) ;n◦r×n " (^) " • Oldest^ field in biochem^ C- late^1700 's)
Coo- Coo^ - OH (^) [ %. Metabolites hare Biocatalysts us^ Over^ Inorganic^ Catalysts^0 Coo^ -^ Various^ potential
Greater reaction (^) specificity ; avoids side^ products decomposition Milder reaction^ conditions^ ; conducive^ to^ conditions^ in^ cells^ Kooi
" -00%4 Enzymes^ make^ the^ desired
Faster (^) reaction rates (^) ; (^) biologically useful timeframe^
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" substrate-f.gs/owreac-1onsllotsol-activation of ) energy barriers^ ↓^ "" ☒aqm⑤qgqp
( G- ± )); surmounted
Enasmesmcreasereac-iionra-esmbyaeorea.mg
substrate entering Enzyme/ Enzyme/
enzyme complex^ complex^ the active site
k=("n±)e×p( -1k¥)
Enzymes :^ Lower^ G-^ ≠ Cyclophilln 10s^ Transition^ state^ #-)
5- substrate Organize reactive (^) groups (close (^) proximity> + proper orientation carbonic (^) anhydrase 10 >^ "É→s f-E-^ product enzyme (^) llncatalyzed biomolecular^ reactions trlosephosphatesomerase.IO"^ ɰÉ-^ -^ -^ -^ -^ -^ -^ HE 2. free reactants → single restricted^ transition^ State^ (entropically carboxypeptidase A^ Ip " É%¥↑!^ Found Transition state -4)
Phosphogklcomutase 10 "^ Reaction^ coordinate
llncatalyzed Uni^ molecular^ reactions succinyl-CoA transferase^ /^ °
rigid transition^ State^ (entropically unfavorable ¥ P Conversion) Urease 10 '^ " reaction catalyzed^ reactions orotidine monophosphate decarboxylase /^ coordinate Enzyme uses (^) binding energy of substrates (organizes reactants^ -1° a (^) fairly rigid ES^ complex Enzyme active^ sites^ (complimentary^ -10^ transition^ state) stronger interactions^ with^ transition^ state^ vs^ ground^ state^ Clower^ Entropy^ cost (paid (^) during binding) activation) Rigid^ reactant^ complex^ →^ (entropically^ neutral^ conversion) Largely AH±^ enthalpy effect^ Enzymes^ bind^ transition^ states^ best