Enzymes Flashcards
Enzymes are
Globular
3D tertiary
Bio catalysts
Biological catalyst
A protein that lowers activation energy
Induced fit
- not perfectly complementary
-AS changes shape by forming weak bonds
-enzyme substrate complex
-changed shape stresses bonds-easier to break
=lower activation energy
Denaturing
Active site changes shape
Bonds holding tertiary structure break
Optimum
Fastest rate of enzyme action
Extracellular enzymes
Digestion
Single celled
Multicelled
Competitive inhibitors
Can be overcome by adding more substrate
Substrate + inhibitor = similar shape
Bind to AT
Blocks substrate- slower rate-less enzyme substrate complexes
Non competitive inhibitors
Different shapes
Allosteric site
Changes AT-tertiary shape =no longer complementary
Slower reaction
Enzyme denatures
Extra cellular enzymes
Secreted out of cell
Amylase in saliva hydrolyses
Starch by breaking glycosidic bonds to maltose (a glucose dissacharride)
And dénaturés in the stomach
Pancreatic amylase is released and
Further hydrolyses starch left
Maltose is hydrolysed to a glucose by
Maltase breaking glycosidic bond in the ileum and the glucose is hydrolysed in cotransport
Denaturing
The bonds holding the tertiary structure of the protein begin to break (this can be for a number of reasons). This causes the active site to change shape as the tertiary structure breaks down. Substrate is no longer complimentary to the active site.
Optimum
Optimum
The conditions at which an enzyme will cause a reaction to occur at it’s quickest rate.
