Karteikarten
Enzymes
Karten in diesem Stapel (15)
- 1Enzymesenzymes lower the activation energy of a reaction
- 2Enzymes- in anabolic reactions enzymes bring the substrate molecules together
- in catabolic reactions the enzyme active site affects the bonds in substrates so they are easier to break
e.g. transferase, ligase and hydrolase - 3Specificity- absolute specificity: the enzyme will catalyse only one reaction
- group specificity: the enzyme will act only on molecules that have a particular functional group e.g. amino acids
- linkage specificity: the enzyme will act on a particular chemical bond
- stereochemical specificity: the enzyme will act on a specific steric isomer - 4Lock and Keyassumes the active site of an enzyme is rigid in its shape
- 5The Induced Fitthe active site is flexible + only assumes it catalytic conformation after the substrate molecules bind to the site
when the product leaves the enzyme, the active site returns to its inactive state - 6Globular proteins- active site has a specific shape due to tertiary shape of the protein
- a change in shape of the protein effects the shape of the active site and the function of the enzyme - 7Characteristics of Enzymesrate of enzyme action is dependent on the number of substrate molecules present
- 8Denaturation- changes in the shape of the enzyme
- temperature
- pH
- radiation
- salt - 9Shape- enzymes must be folded into the right 3D shape to function
- enzymes are suited to function best with a certain temperature, pH ect
- denaturation is a process in which proteins lose their quarternary, tertiary and secondary structure
- this is caused by application of external stress
- if proteins are denatured cell activity is disrupted - 10Enzyme regulation- enzymes can be regulated to promote or reduce activity
- sometimes an inhibitor molecule is similar enough to a substrate that it can bind to the active site and act as a block
- other times the inhibitor binds to the allosteric site
- some inhibitors can change the shape of the enzyme so the substrate is less likely to bind. - 11Competitive Inhibitors- work by preventing the formation of enzyme-substrate complexes as they have a similar shape to the substrate
- they fit in the active site but remain unreacted . this causes the reaction rate to decrease
- usually temporary - 12Non-competitive Inhibitors- bind to the allosteric site causing the structure to distort
- not affected by substrate concentration
- many are irreversible and permanent
- non-permanent ones are responsible for controlling metabolic functions - 13Regulation- many enzymes do not work optimally unless bound to a non-specific helper molecule
- temporary bond: ionic or hydrogen bonds
- permanent bond: covalent bond - 14Cofactorinorganic ions
- 15Coenymesorganic helper molecules (basic atomic structure)
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- Biology Karteikarten am Enzymes, erstellt von Ellie august am 25/10/2025.
- Erstellt von
- Ellie august
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