FACTORS AFFECTING ENZYME ACTIVITY

INCREASE - INCREASE ENZYME ACTIVITY

- MOLECULES VIBRATE MORE

TOO HIGH
- BREAK HYDROGEN/IONIC BONDS - OR DISULFIDE BRIDGES
- CHANGE ACTIVE SITE
- SUBSTRATE NO LONGER FIT

- DENATURE ENZYME

OPTIMUM pH VALUE = 7 (NEUTRAL) - HUMANS

PEPSIN - STOMACH - pH VALUE = 2 (ACIDIC)

ABOVE OR BELOW OP. PH
- HYDROGEN AND HYDROXIDE IONS
- MESS UP HYDROGEN AND IONIC BONDS - AFFECT TERTIARY STRUCTURE

CHANGE ACTIVE SITE SHAPE
- DENATURE ENZYME

HIGHER CONC - HIGHER RATE OF COLLISION
- MORE ENZYME MOLECULES
- MORE E.S.C FORMED
- R.O.R INCREASE

LIMITED
- EFFECT DEPENDS UPON AMOUNT OF SUBSTRATE AVAILABLE
- NO MORE - NO FUTHER EFFECT

HIGHER - FASTER R.O.R
- MORE COLLISIONS
- MORE ACTIVE SITES USED

ONLY TRUE - UP TO SATURATION POINT
- ALL ACTIVE SITES FULL
- NO FUTHER EFFECT

SUBSTRATE CONC- DECREASE - OVER TIME
- NO OTHER VARIABLE CHANGE
- R.O.R DECREASE OVER TIME
- INITAL R.O.R - HIGHEST

COMPETITIVE MOLECULES = SIMILAR SHAPE TO SUBSTRATE

- COMPETE WITH SUBSTRATE FOR ACTIVE SITE
- NO REACTION TAKES PLACE

BLOCK ACTIVE SITE
- NO SUBSTRATE CAN BIND

HIGH CONC OF INHIBITOR
- MORE ACTIVE SITES OCCUPIED
- FEW E.S.C

HIGHER CONC OF SUBSTRATE
- INCREASE R.O.R
- GET TO ACTIVE SITE QUICKER

NON-COMPETITIVE MOLECULES - BIND TO ENZYME AWAY FROM ACTIVE SITE

ACTIVE SITE CHANGE SHAPE
- SUBSTRATE MOLECULES CANT BIND

- DONT COMPETE - HAVE DIFFERENT SHAPE TO SUBSTRATE

- INCREASING SUBSTRATE CONC. - NO DIFFERENCE