enzymes 2.1.4

Alternative transcript:

of readin L> change in 3D structure of enzyme so can no longer bind to substrate a дети Ea without enzyme Ea with enzyme change in free energy AG energy in the enzymes Factors Affecting Enzyme Action 4) measure rate of formation of product L> Measure dissaperance of Extracellular Enzymes substrate -enzymes released from. boccurs in the gub -cells Denaturation <shigh temp. bonds L> secreted by gungi / holding molecules together -> OPTIMUM Temp. vibrate more -temp. at which greatest has ROR 4shumans = 40°C garmed L>: increases rate greaction -temperature coefficient = Q₁0 4> measure of how RoR increases 4> Thermophilic bacteria = 70°C²° paychophilie organisms = 8=X<5°C Effect of pH longer complimentary C>: denatured enzyme L> NON-Reversible with a 10°C rise in temp. -H bends & Tonic bonds between amino enzyme controlled reactions acid R groups hold proteins in precise 3D shape Ly usually taken as '2'` - the more H² ions present, less R groups are able to interact L> Rok doubles with 10°C rise with eachother -> bonds freak -> enzyme shape changes. enzyme - signigigaub ph chougе -> donatives irreversibly the shape of the - very nourou pH renge for a given enzyme <> lead to breaking bonds L>can change 3D shape of active site L> substrate = no an enzyme substrate complex Enzymes L> competature inhibiters. non competitive intubitions. Key Words -cogacter -coenzyme - prosthetic group - allesteric site -competetive -non-competetive Linhibiters - tertiary structuure - reversible -non-reversible - concentration - precursor activation L>zymagurs L> pro-enzymes - negative feedback control L> cofactors L> coenzymes Enzyme Inhibitors -competitive - Substrate -non-competitive Non-Competetive Inhibitor + prosthetic group -blocks the formation of an enzyme substrate complex -Substrate & intuebiter molecules compete to bind to the active site -Inhibiter binds at a site other L> most compeletive inhibiters only temporainly bind = REVERSIBLE than the active site allosteric site. V max Enzymes = negative -causes change in tertiary structure -substrate can no-longer bind to the active site og - Increasing the concentration. enzyme / substrate will not overcome the effect: NON-REVERSIBLE - Increasing the concentration inhibitor will decrease rate te of • Competetive inhibiteer. - molecule with a similar shape to the substrate - Required by certain enzymes to carry out catalytic gunchan -tightly bound & permanent geature Le g Zinc carbonic anhydrose L> metabolism of CO₂ un Summary -competetive inhibiter reversible of of change tertiary structure can be brought about by action another enzyme (protease) c) cleaves bond in molecule change in environment L>pH or temp. L> change in tertiary. structure + activation - non-competative inhibitor non-reversible -cofacters obtained via diet as minerals -coenzymes: derived vitanins igrom L>zymogens & proenzymes Czeg pepsinogen->pepsin absence of unnibitor Cogacters & Coenzymes. -non-protein components. reaction further L>transfer atems or groups from 1 reaction to another in a multi-step pathway / may form part of the active site - 1g cofactor = organic indecule = COENZYME Coenzymes - Examples include organophosphates Labind to acetyl cholinesterase Inorganic Cogacters L>needed ger synapses - death 1-denred from vitamins-obtained via deet as minerals. 4>83 = synthesis of NAD Leg Ct ger amylase Prosthetic Groups L>BS = coenzyme A L> correctly shaped acture site. fixed of competet unhibitor gired quantity o incubitors substrate concentration apoenzyme inactive OCR 12/13 cofacter 2.1. enzymes feedback control L> non-competetive reversible. inhibition Lexcess product NOT made A resources NOT wasted. Precursor Activation enzymes produced in mactive form Lunderge change in shape. L>e. ∙9 active site to be activated -achieved by addition of a co-facter Lse.g enzymes that could damage cells producing them cictivation -coenzyme substrate новенчуте active can band to allosenc site, needed for efficient enzyme gunction