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specific protein that is synthesized by the cell under direction of DNA.


vitamin derivative. not made by the cell, but must get from diet.


when the apoenzyme has all three slots filled: allosterik sites have co enzyme and inorganic co factor as well as the active site having substrate.

turnover number

the number of molecules of substrate converted to product per unit of time

environmental factors affecting enzyme activity

temperature, pH, and concentration

doubling effect

the turnover number doubles with each 10 degree increase up to the optimum temperature.

examble of doubling effect: if an enzyme at 20degrees C the turnover number is 100----

0 degrees=25**10 degrees=50*20 degrees=100**30 degrees= nothing, denaturization

pH effect on enzyme

every enzyme has an optimum pH. greater than +/- 3 on the pH will lead to denaturization.

4 principles of complete inhibition

1. both the substrate and the inhibitor must be chemically similiar. 2. the enzyme can react at the same rate with either the substrate or the inhibitor. 3. whichever is present in greater concentration(substrate or inhibitor) determine the degree of inhibition. 4. must be clinically reversible inhibition.

non competitive inhibition

the inhibitor goes to one of the allosterick sites. the advantage is that less inhibitor is needed. permanent or long lasting.

biochemical pathway

series of enzyme catalyzed reactions

oxidation reaction

electron transfer reaction


the cofactor is the activator. together, the apoenzyme and cofactor form a holoenzyme. if the cofactor is removed, the apoenzyme will not function.

active site

found on the surface of the enzyme. receives a specific substrate.

allosterik sites

also found on the surface, but accept the co enzyme and the cofactor.


a specific substance which catalyzes a reaction in an enzyme.


total irreversible loss of all activity.

name the six high-energy compounds


what is ETS?

Electron Transfer System, aerobic only, series of redox reactions initiated by the presence of NADH₂ or FADH₂, occurs (1) in the cell membrane of prokaryotic cells and (2) in the mitochondria of eukaryotic cells

CO₂ Rule

under aerobic conditions, each C-atom in the original substrate will yeild 1CO₂

NADH₂ in fermentation

the NADH₂ always goes Lactogenesis

NADH₂ in anaerobic respiration

the NADH₂ always goes METS

anaerobic respiration never makes.....


Fatty Acid under aerobic conditions

fatty acid goes through beta oxidation

Fatty Acid under anaerobic conditions

fatty acid goes through NOTHING...there is NO catabolism of fatty acid, it goes right to the cell membrane

Metabolic Fates of amino acids

(1) reassembles into cellular proteins and apoenzymes (2)production of purines (adenine and guarine) and pyrimidines (thymine, cytosine, and uracil). (3)peptidoglycan syntheis (4) other synthesis reactions (5) catabolism of amino acids. 1-4 are anabolism.

Pasteur Effect 1

(1) organisms are MOST EFFICIENT REPRODUCTIVELY under AEROBIC conditions (lots of ATP) and MOST EFFICIENT in the formation of CHEMICAL BYPRODUCTS (lactic acid, ethanol, and inorganic acids such as sulfuric, nitric and carbonic) under AEROBIC conditions.

Pasteur Effect 2

this applies to all facultative anaerobes.

medical application of Pasteur Effect

Staphylococcus Aureus (facultative anaerobe) In aerobic infection--->losts of pus (50% cells) and very little toxin formation---> antibiotics to treat. In anaerobic infection--->very few cells and lots of toxin--->antibiotics are useless

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