Enzyme Biochem 1 Fn

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Commonly Active sites can be

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Bound metal ions (Mineral) -- Bound organic groups (vitamins) --- Specific amino acids

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Co-enzyme vs Co-factor

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Organic (Vitamin) vs Inorganic (Ca-P)

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Apoenzyme (inactive)

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ezn wo its prostethic group or metal group (co factor)
vitamin (coenz) and prostethic ezn (permanent -- heme)

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1. Oxido-reductase --- FAD - riboflavin B2

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Add or remove electrons (and commonly also hydrogen) ---

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2. Transferase: Norepi -- Epi - CH3

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Transfer one group from one molecule to another -- CH3

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3. Hydrolase: Asparagine (NH3) --- Aspartate (COO)

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Hydrolysis of functional group by water

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4. Lyase: HMG-CoA ---- Acetoacetate (double bond)

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Addition or removal of double bonds when adding or removing a functional group

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5. Isomerases: G3P --- DHAP

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changing to new isomer

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6. Ligase: Glycine - GAR

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Creates C-C, C-N, C-O, C-S bonds usually with the assistance of ATP

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Michaelis-Menten plot can predict and calculate Km - Vm base on substrate concentration

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use 1/S ---> x-int= -1/Km ----- y-int= 1/Vm ----- slope = Km/Vmax (reciprocal of Km/Vm)

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Km

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is the concentration of substrate that half saturates the enzyme. The lower the Km the higher the affinity of the enzyme for the substrate

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Kcat

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is how fast this enzyme can go compared to other enzymes

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Find Km

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Find Vm = 647 --- Calc 1/2 Vm = 325 ---> determine Km= 2nM (conc substrate needed to be 1/2 Vm)

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Suicide inhibitor

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Suicide enz bind and inativate the act of enz --> not letting go --> Aspirin acetyl bind into

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covalent modification

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Phosphorylation

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Enz cooperativity (Positive and negative regulation)

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Vmax is the same --- can increase of decrease Km

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Competitive Inhibition: Methotraxate (cancer) bind to DHFR (DNA synthesis) and compete with folic acid B9 to inhibit DNA synthesis

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Amt of DHFR is unchange (V max is the same) ---- if Meth increase (while Vm same) need MORE DHFR (substrate conc=Km) to have the same speed of action ----------------- if conc inc -----> Slope inc --- Vm same - Km increase

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Un-competitive Inhibition (un --- parallel)

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Inibitor binds only after substrate has already bound, but slows down conversion to product. ----- CONC inc --> Slope same --- Vm dec - Km dec (1/2-1/3)

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Mixed Inhibition --- tert Comp

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Inhibitor binds at any time -- CONC inc ---> Slope inc --- Vm dec - Km increase

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Non-competitive Inhibition

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CONC inc --> slop inc ----- Vm dec ---- Km same

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Ternary Complex ---- mixed

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random order -- order both sub bind the same time --

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Ping-Pong Kinetics ---- un--compete

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1st bind first then 2nd come in --> ATP first to bind P then glucose come in to use P parallel

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Name some of the common amino acids and other “non-amino acid” chemicals that can be found at an active site.

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Glu-Asp ----- Lys-Arg ----- Cys ---- His -------- Ser ----- Tyr

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Feedback Inhibition

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s the product of many the rxn down the line to stop the beginning rxn (to save energy to make too many middle guys)