Enzymes at Fachhochschulstudiengänge Krems IMC | Flashcards & Summaries

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Function enzymes: general (5)

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- bio-catalysts (accelerate biochemical processes) -> lower activation energy (delta G must be negative so a reaction works)

-are proteins

-high specificity (for substrate and reaction)

-can transform one energy into another one

-do NOT change chemical equilibrium of chemical reaction but increase reaction rate in both directions



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Units of enzyme activity

- 1 katal / 1 kat

- 1 unit (1 U)

- turnover number

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- 1 katal / 1 kat (Conversion of 1 mol substarte / sec) (µkat, nkat)

- 1 unit (1 U) (Conversion of 1 µmol / min)

- turnover number (µmol substrate / (min. µmol enzyme)) (like vmax/amount of enzyme)

 -> can get it from vmax, number of substrate converted in product in  one unit of time)

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Action of inhibitors:

- 6 types

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- Irreversible inhibition

- reversible inhibition

- product inhibition


-competitive inhibition

-non-competitive inhibition

-uncompetitive inhibition (mixed)

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Different types of enzyme regulation:

self- regulation

-> by?

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- substrate concentration


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Different types of enzyme regulation:

-covalent modifications

-> how?

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- covalent attachement of chemical group

-for example phosphorylation (ATP) or acetylation (Acetyl CoA)


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Different types of enzyme regulation:

-phosphorylation

-> from which molecules?

-which charges for one phosphoryl groups

-new bonds?

-closely linked to ?

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- ATP or GTP like a switch (activated/ deactivated)

- two negative charges are added per phosphoryl group

- novel hydrogen bonds / ionic interactions

- closely linked to energy status of the cell

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Enzymes (energetic)

-chem. equilibrium

-what does the activ. energy lowering lead to?

- what does the free energy of activation (delta G ++) determine?

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-satet of lowest gibbs free energy (delta G) -> no work performed

-increases probability of reaction significantly

-the rate of the reaction


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Enzyme Regulation: 

proteolytic activation

-what?

- how?

-but?

-inactive precursors

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TESTE DEIN WISSEN

irreversible conversion of inactive to active enzyme

- via proteolytic cleavage

- but: inactivation of active enzymme can still occur by binding inhibitors

- precursors: Zymogen, proenzyme 

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Interaction between substrate and enzymes (5)

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-H2-bonds

-ionic interactions

-electrostatic forces

-hydrophobic forces

-formation of transient covalent bond

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Classes of enzymes (7)

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1. Oxidoreductases

2. Transferases

3. Hydrolases

4. Lyases (form DBs)

5. Isomerases

6. Ligases (Ligation of 2 substrates at expense of ATP)

7. Translocases 


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Isoenzyme?

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-catalyse same enzymatic reaction

-found in different cell or tissues

- frequently regulated in diff ways

- products of diff genes

-diff in physical, chemical and CATALYTIC prop.

-separated by conventional methods like electrophoresis

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4 basic mechanisms of enzyme catalysis

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-> use one or more of these strategies!


1. Covalent Catalysis (temp covalent bond in active site)

2. General Acid-Base Catalysis (crucial proton donotor or acceptor)

3. Catalysis by approximation (bring two substrates close together in right arrangement to enzyme)

4. Metal ion catalysis (promotes formation of Nu-/E+ -> bridge between enzyme and substrate)

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Q:

Function enzymes: general (5)

A:

- bio-catalysts (accelerate biochemical processes) -> lower activation energy (delta G must be negative so a reaction works)

-are proteins

-high specificity (for substrate and reaction)

-can transform one energy into another one

-do NOT change chemical equilibrium of chemical reaction but increase reaction rate in both directions



Q:

Units of enzyme activity

- 1 katal / 1 kat

- 1 unit (1 U)

- turnover number

A:

- 1 katal / 1 kat (Conversion of 1 mol substarte / sec) (µkat, nkat)

- 1 unit (1 U) (Conversion of 1 µmol / min)

- turnover number (µmol substrate / (min. µmol enzyme)) (like vmax/amount of enzyme)

 -> can get it from vmax, number of substrate converted in product in  one unit of time)

Q:

Action of inhibitors:

- 6 types

A:

- Irreversible inhibition

- reversible inhibition

- product inhibition


-competitive inhibition

-non-competitive inhibition

-uncompetitive inhibition (mixed)

Q:

Different types of enzyme regulation:

self- regulation

-> by?

A:

- substrate concentration


Q:

Different types of enzyme regulation:

-covalent modifications

-> how?

A:

- covalent attachement of chemical group

-for example phosphorylation (ATP) or acetylation (Acetyl CoA)


Mehr Karteikarten anzeigen
Q:

Different types of enzyme regulation:

-phosphorylation

-> from which molecules?

-which charges for one phosphoryl groups

-new bonds?

-closely linked to ?

A:

- ATP or GTP like a switch (activated/ deactivated)

- two negative charges are added per phosphoryl group

- novel hydrogen bonds / ionic interactions

- closely linked to energy status of the cell

Q:

Enzymes (energetic)

-chem. equilibrium

-what does the activ. energy lowering lead to?

- what does the free energy of activation (delta G ++) determine?

A:

-satet of lowest gibbs free energy (delta G) -> no work performed

-increases probability of reaction significantly

-the rate of the reaction


Q:
Enzyme Regulation: 

proteolytic activation

-what?

- how?

-but?

-inactive precursors

A:

irreversible conversion of inactive to active enzyme

- via proteolytic cleavage

- but: inactivation of active enzymme can still occur by binding inhibitors

- precursors: Zymogen, proenzyme 

Q:

Interaction between substrate and enzymes (5)

A:

-H2-bonds

-ionic interactions

-electrostatic forces

-hydrophobic forces

-formation of transient covalent bond

Q:

Classes of enzymes (7)

A:

1. Oxidoreductases

2. Transferases

3. Hydrolases

4. Lyases (form DBs)

5. Isomerases

6. Ligases (Ligation of 2 substrates at expense of ATP)

7. Translocases 


Q:

Isoenzyme?

A:

-catalyse same enzymatic reaction

-found in different cell or tissues

- frequently regulated in diff ways

- products of diff genes

-diff in physical, chemical and CATALYTIC prop.

-separated by conventional methods like electrophoresis

Q:

4 basic mechanisms of enzyme catalysis

A:

-> use one or more of these strategies!


1. Covalent Catalysis (temp covalent bond in active site)

2. General Acid-Base Catalysis (crucial proton donotor or acceptor)

3. Catalysis by approximation (bring two substrates close together in right arrangement to enzyme)

4. Metal ion catalysis (promotes formation of Nu-/E+ -> bridge between enzyme and substrate)

Enzymes

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