Chapter 7: Enzyme Mechanism of Action Notes, Summaries of Biochemistry

Download Chapter 7: Enzyme Mechanism of Action Notes and more Summaries Biochemistry in PDF only on Docsity! Enzymes:MOA Prosthetic groups/copactor/coenzymes Enzymes :catalystof high MOA 5Biological origin ↳extend mechanistic capabilities by penal groups - catalyze cheminen - rRNA present on the aminoacyl side chains of peptide almostall are protein exceptkibozymes 5 RNAwI endonuclease/nucleotide ligase Prosthetic Groups: -incorp by covalent /n-covalent * Protease rentin-cheeses A pyridoxal phosphate lactase- remove lactose from milk Marin mononucleotide Protease & Amylase - removes stains RAD iamine pyrophosphate - Enzymes can catalyzed substrates to product Lipoic acid ↳ rate 104 or 110 Biotin ↳ Transient alteration -> enzyme Transition m. (Pe,Cr,cr,M9,Mn,(n) modification - By acting as Lewis acid/base 4 Selective a specific 4 at least 3 points attachmentco-pactors:operational ↳ Chiral to non-chival :Bind weakly -> disociable complexes :mustbepresentin envi to promote Eq. pyruvateTL-laltate pormation lactate dehydrogenase :metal:metal-activated enzymes - *metalloenzymesandmetal ions classified by reaction type as prosthetic groups ·-ase as supeix 0 oxidoreductase - Redox perivatives a Vitamins: & Transperses - transper of moieties e.g. methyl · nicotinamide - NAD & NADP ⑧ Adrolases - hydrolytic clearage of coventbonds · Riboplavin - redox of coenzyme RMNGRAD e.q.c-c/c-0/2 -N · Pantothenic acid-COA · Miamin - decarboxylation as X-ketoacids & lyases - catalyze cleavage on C-2/c-8/c-N · Rolic Acid d - one-carbon metab ↳ atom elim. -> making a DOUBLEBOND cobamide 6 Isomerase - catalyze geometric/structural coenzymes as substrate shuttles - changes win a molecule ↳recyclable shuttles ken:O stabilize species thatare too reactive ·g. RADH, or Hydride Ions(NADH) ⑧lipase - catalyze joining together (ligation) ↓ hydrolysis or ATP & increase to points of contactA substrated enzyme -> ↑ appinity a specificity E.g.COA, glucose (VDP) 1 hydride (NADY) catalysis at active site ↳ E + s ->Is complex ↳ingmechanism ↳ Fischer:Lock &Keymodel - Astsubs Bound- product released · Has active site - site por recognition prior to binding to2nd - sitefor envi where chem' transformation substrates Induce conformational changes in Enzymes takes place ↳ Roshland's induced it model - optimal alignment - s+E -> conformational change -chield substrates t -Enzymes induces reciprocal change harnessing Iwater Energy op binding mechanistic strategies topacilitate catalysis HIV Proteases -> Acid Base Catalysis (A-B catalysis) ↳aspartic protease pamily (pepsin,lysosomal cathepsins) :Catalysis by proximity ↳ a AIV - Bond-forming distance use 2 concerve asparty residue for ↑ Cone4 Preq. op encounter ratea ran A -B catalysis ↳ ↑ local substrate concentration Stage 1:Aspartate as general base (Aspx) 4 rate atatleast1000x ↓ - gets it from 120 - 120 more direct nudeophilic c. Acid-Base catalysis mycitygetit ↓ -xn for as only participating acids attacks electrophilic or bases are protons/hydroxide ions Tetrahedraltransite- carbonyl carbore - Rate on ran is sensitive to changes of ↓ peptide tar. by hydrolysis cone butindependentothe cone. 2"Aspartate (Asp7) -General And/General Base Catalysis Facil decomposition -> rupture a -> shuttling ↳ rate resp. to all adds or bases qc tetrahedral by peptide ↓ donating At r bord restors protease to 3. Catalysis by strain amino group initial stage "involves breaking a covalentbond ↳weaknes band targeted by cleaval COVALENTCATALYSIS though physical distration a electronic polarization · Chymotrypsin - serine protease chymotrypsin stained -> Transition State Intermediate involves formation of covalent ↳ midway acyl-enzyme intermediate "Transition State stabilization -gen much wil > Asp 102- His 57-Ser195 Proton ⑦ accelerate rate ↳charge-relay network -> shuttle achem non ser 195-***D2-04 -Act-erm 4 Covarent catalysis (A nucleophilicityintermediate - modified e -> reactanta new pathway wk Ea is lower - pormation of covalent bond * enzyme /substrates ·onthe↓ leaves - AA ↳ Transient - remain, Pastryth activesite ↳Common togroup transper ran I replacedbyHite Or4. Residues are: cys/Ser/His.