Biochem: Enzymes

Ligase

Join molecules together, typically requires an ATP

Isomerase

Rearranges the to the other enantiomer

Lyase

Breaks compounds apart

Hydrolase

Breaks compounds apart via water

Oxid0-reductase

Transfers electrons (Redox)

Transferase

Transfers functional groups (ie kinase)

Vmax

Maximum rate at enzyme saturation

Km

Substrate concentration at ½ vmax

closer to 0

Which has a higher Km value

Lower y-intercept

Which has a higher Vmax

Competitive inhibitors

Increase km, doesn't change vmax

Non-competitive inhibitors

Doesn't change km , decrease vmax

Uncompetitive inhibitors

Decrease km, decrease V max -parallel

Mixed inhibitors

Two options - both decrease vmax

Inhibitor prefers binding to enzyme -substrate complex

Decrease Vmax, decrease km

If inhibitor prefers binding to enzyme alone

Decrease vmax, increase km

Cofactors

Generally inorganic molecules, metal ions, and are often ingested as dietary minerals

Coenzymes

Small organic grapes, and the mass majority of which our minerals are derivatives of vitamins, such as NAD+,FAD, and coenzyme a

Apoenzymes

Enzymes without their cofactors

Holoenzymes

Enzymes with their cofactors

Prosthetic groups

Tightly bound cofactors/coincides that are necessary for enzyme function

Catalytic efficiency

kcal/Km, how well an enzyme converts substrate to product

Hills coefficient

>1; positively cooperative binding

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