Biochem Enzymes

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Enzymes play an important role in

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-Metabolism

-Diagnosis

-Theraputics

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All biochemical reactions are enzyme catalyzed in

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Living Organisms

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Can enzymes be use theraputically?

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Yes

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Disease that has relation with enzyme indication

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Myocardial Infarction

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Cleaves viral polyprotein

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Protease

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Synthesizes RNA into DNA

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Reverse Transcriptase

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Enzyme classes

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-Oxidoreductases

-Tranferases

-Hydrolases

-Lyases

-Isomerases

-Ligases

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Alchohol dehydrogenase

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Oxydoreductase

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Oxidation with NAD+

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Oxydoreductase

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Hexokinase (phosephorilation)

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Transferase

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Carboxypeptidase A (Peptide Bond Cleavage)

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Hydrolases

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Pyruvate Decarboxylase (Decarboxylation)

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Lyases

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Maleate Isomerase (Cis-Trans)

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Isomerases

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Pyruvate Carboxylase (Carboxylation)

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Ligases

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Greatly incrase the rate of chemical reactions

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Enzymes

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Typically help to transform one energy form to a more usable form

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Enzyme

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Enzyme do not act alone they require

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Helper Molecule

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Enzymes are highly

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Specific

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Types of enzyme specificity

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-Absolute

-Group

-Linkage

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Catalyze one type of reaction for a single substrate

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Absolute

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Catalyze one type of reaction for similar substances

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Group

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Catalyze one type ofreaction for a specific bond

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Linkage

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True or false wnzymes amount will be the same before and after the reaction

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True

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Enzymes are

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Proteins

Catalyst

Enters reaction but not consumed

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Amount of energy that must be supplied in order to keep the reaction going

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Activation energy

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It is the apex of the curve which is the energy that drives the transition state

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Activation energy

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Enzymes lower down----- by stabilizing the transition state

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Activation energy

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Enzymes lower down activation energy by stabilizing the

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Transition state

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Substrate binds to specific regions of enzymes called

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Active Site

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Stabilizes the transition state

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Active site

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Active site binds substrate---- via non-covalent bonds

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Reversibly

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Active site binds substrate reversibly via

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Non-covalent bonds

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Two models of enzyme action

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Lock-and-key model

Induced Fit Model

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The active site has rigid shape wherein only substrates with the matching shape can fit and it is an older model that does not work for all enzymes

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Lock-and-Key Model

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The active site is flexible wherein the shapes of the enzyme,active site, and substrate adjust to maximize the fit which improves catalysis

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Induced Fit Model

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The inhibitor binds to the enzyme irreversibly throughformation of a covalent bond with the enzyme permanently inactivating the enzyme

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Irreversible inhibition

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What affects enzyme activity

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Enviromental Conditions

Cofactors and Coenzyme

Enzyme Inhibitors

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Ideal pH of enzymes

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6-8

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The tempearture at which enzymatic reaction occurs fastest

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Optimum temperature

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Major alchohols esterified to phosphatidic acid to form glycerophospholipids

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Choline

Ethanolamine

Glycerol

Inositol

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Muscle enzymes

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Creatinase

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) is a system of classifying enzymes based on their functions. It also assigned corresponding codes for these enzymes

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IUB

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Enzyme in HIV

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Reverse Transcriptase

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medication used to combat HIV/AIDS. Targets enzymes that needed to undergo reverse transcription process

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Azidothymidine

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Enzymes which is important for the survival of HIV

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Protease

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Used to destroy protease

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Saquinavir

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Oxidation (to reduce or oxidize compounds) Acid and bases Transfer of electron and hydrogen atoms Example: alcohol dehydrogenase

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Oxidoreductases

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 To transfer (or to move) functional groups within the molecules

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Transferases

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 Addition of H+ and small molecule like water to break down the bonds or convert the compounds into smaller pieces (condensation reaction)  Example: carboxypeptidase A

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Hydrolases

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Almost same with hydrolases  Breaks down compounds into smaller pieces without presence of water  Example: Pyruvate decarboxylase

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Lyases

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Rearrangement of atoms within a molecule  Isomerization  Example: maleate isomerase (cis-trans isomerization)

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Isomerases

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“Synthetases”  Join, form or synthesize compounds  Example: Pyruvate carboxylase

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Ligases

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Enzyme alone

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Apoenzyme

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helper molecules; promote, enhance or activates the enzyme; can be classified into organic (cofactor as specifically “coenzymes”) or inorganic compounds (simple metal ions

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Cofactor

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complete enzyme (combination of apoenzyme and cofactor); ready to catalyze chemical reactions

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Holoenzyme

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The curve when reaction rate did not exceed the Vmax (the curve level offs before the Vmax)

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Asymptotic curve

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if the rate is directly proportional to the [S] (the activity of enzyme increases while conc. of substrate is added)

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First order reaction

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– if Vmax is reached, it does not exceed to Vmax even you add more substrate conc. (constant reaction)

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Zero Order Reaction

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Rate of formation

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ES =K1 [E] [S]

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Rate of Dissociation

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ES= K-1 [E] [S] + K2 [E] [P]

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Standard Unit of Enzme Activity

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Katal

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Inhibitor resembles the shape of the actual substrate  Prevents from binding the active site

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Competitive Inhibition

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Competitive Inhibition can be resolve by

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Increasing the number of substrate

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The binding of S to the active site creates a crevice/pocket called Allosteric site – additional active site; not found initially; inhibitors create a new or additional active site  If it is in close proximity with the ES complex, then this will prevent the S from dissociating from the active site

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Uncompetitive Inhibition

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Cannot be overcome by increasing substrate

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Uncompetitive Inhibition

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Allosteric site is already present before substrate binds to the active site o Regardless whether there is substrate or no substrate (at first)

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Noncompetitive Inhibition

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Increases Km, Vmax is unaffected

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Competitive Inhibition

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Decreases both Km and Vmax = parallel

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Uncompetitive Inhibition

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Decreases Vmax, does not affect Km

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Noncompetitive Inhibition

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occurs when the enzyme is saturated (when all enzymes are binding substrate)

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Maximum Activity