Unformatted text preview: product
ii. Binding to active site is an energonic chemical reaction
- Independent chemical reaction - This specific binning powers induced fit and strains bonds of substrates to increase order and decrease enti'opy
iii. Enzyme operatfi through two steps
One Enzyme binding
Two. {:atalysis I. Enzyme's effect on chemical reactions
A. Gibbs tree energy diagram A. Effecls
1. EI'IZ'HTIE lower M5“, and increase k {rate constant]
1. lncreaseofkbyalot
a} Small decrease in energy ofactiyation? Magnitudes ofgreater
reaction Hates
i. Ex. Catalase -: 1 billion times larger reaction rate for the
decomposition of hydrogen peroxide
Increases the rate by same amount for forward and reverse reactions
Rate in both directions still dependent on concentmtion of both substrate and
product
1. Most reactions freely proceed in both direction
a} Thus they are substi'a‘le—prochct concentration driyen yia Le
Chatelier's principle
4. Enzyme does not affect position of equilibrium; :56“ dog not change; It:Ell does
fit charge 55“!“ I. Triose Phosphate Isomerase - Reaction Mechanism [Acid base mtalysis]
A. Not in tailback.
E. Additional reading on TED MebCT] 1. I'm — Need to do proton and electron pushing arrows
C. Triose phosphate isomerase is an enzyme that functions in glycolysis
1. glucose {6 carbon] is cut into two 3 carbon molecules
1. Dihyrioxyacetone phosphate [DHAP] into glyceraldehydeS-phosphate
IGBPJ
2. TPI catalyzes DHAP .2 car
3. Extremely reversable in both directions E‘FM 'L‘ _‘ fibril-INF}: Cadill- ill; 12:"; "=9” as 33> ETHC if!" Fan: 15 ...
View
Full Document
- Spring '08
- Price
-
Click to edit the document details