Enzymes

aksh and ronnan are banned from this knowt

Enzyme

Enzyme

Proteins

Monomer=amino acids

Polymer=polypeptide

Function=Regulate(speed up) chemical reactions

Metabolic Processes

• Activation energy→ the amount of energy needed to trigger the formation of new bonds

• Catalyst→ help to speed up reactions

  • Lower activation energy

  • They are reused

how enzymes connect to life

we could wait for reactents to to randomly come but we are large complex species and would never evolve

Enzymes and life: chemical reactions

Transition state : reactants have absorbed enough energy to break apart and reform as products. 

activation energy: input of energy required for reaction to occur.  

substrate

• The substance the enzyme acts upon

  • Ex: Salivary amylase is the enzyme that breaks down the substrate starch

substarte specific

•  They only work with particular substrates, they are not interchangeable

active site

• The location where substrates and enzymes attach

Induced fit model

the location where substrates and enzymes attach

Enzymes end in

ase

What Can Change an Enzyme?

• Changes in temperature or pH can cause denaturation of the enzyme

• They can be repaired as long as their primary structure stays intact

Structure = Function

• The way a protein folds determines its shape which determines its function

  • When the shape of a protein changes it no longer holds the same function

• How does the shape change?

  • High temperatures

  • Changes in pH

  • Mutations in the genetic code

Denaturation

Changing the SHAPE of the enzymes

Specifically changing the shape of the active site 

When the active site changes shape, the specific substrate no longer fits

what are the affects of the cold

• Cold temperatures make everything SLOWER

  • The reaction still happens but the reaction rate significantly decreases

Allosteric enzymes

• Activator→ binds and induces ACTIVE form

• Inhibitor → binds and induces INACTIVE form

Feedback inhibition

•  the end products of a reaction act as inhibitors

  • Aka a negative feedback loop

Competitive inhibition

•  a molecule mimics the substrate and occupies the active site

• The reaction cannot proceed

Noncompetitive inhibitor

• a molecule binds somewhere that is NOT the active site or allosteric site

Cooperativity

• an enzyme allows more substrates to bind after the first one has bound

  • The enzyme must have 2+ subunits for this to occur