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proteins that are a catalyst of biochemical reactions. Enzymes are not permanently changed by the chemical reactions they catalyze |
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The reactant that binds to an enzyme and it will be converted into a product. |
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The final molecule(s) that result from the enzyme catalyzed biochemical reaction. |
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The amount of product produced per unit of time. |
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the region of the enzyme where the substrate binds and the biochemical reaction occurs. |
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Some enzymes require an additional non-protein prosthetic group to function (same as complex protein). The polypeptide portion of such an enzyme is called the apoenzyme. |
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(non-protein portion) are ions or smaller organic molecules needed for the activity of specific enzymes. Some cofactors include metal ions such as Ca2+, Mg2+ and Cu2+. |
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(non-protein portion) are organic molecules derived from niacin, riboflavin, and other water soluble vitamins. They are needed for the activity of specific enzymes. |
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the complete enzyme-cofactor complex that gives full catalytic activity. |
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materials that reduce the catalytic activity of an enzyme. |
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inactive enzyme precursor |
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structurally related protein products of different genes that catalyze the same biochemical reaction. |
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biochemical reactions that share a common intermediate. |
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catalyzes the transfer of groups such as amino, carboxyl, glucosyl, and methyl. This does not include water. |
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Catalyze oxidation/reduction reactions. |
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Catalyze hydrolysis reactions. |
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Catalyzes the covalent bonding of two molecules coupled with the hydrolysis of high energy bonds in ATP or similar compund. |
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Catalyzes the introconversion of structures or geometric changes in a molecule. |
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Catalyzes the formation of double bonds or reactions involving double bonds |
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digests starches to disaccharides (two simple sugars) |
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further digests dietary fats into fatty acids and glycerol. |
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involved in the emulsification process of lipid absorption. |
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can either preak specific peptide bonds depending on the amino acid sequence of a protein, or break down a complete peptide to amino acide. |
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an alkaline secretion which neutralizes the acitid gastric juice as it enters the small intestine. |
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inhibitors that directly compete with the substrate for binding within the enzyme active site. |
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Noncompetitive inhibitors |
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weakly bind to an allosteric regulatory site on the enzyme such as a cofactor binding site. Does not compete with substrate for active site. |
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the principle pigment in bile derived from the breakdown of hemoglobin. |
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a complication of many liver diseases that is characterized by abnormal structure and function of the liver. |
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discharge of waste from an organ (Liver). |
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process by which substances are released fro an organ for a specific purpose. |
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an inflammation of the liver often caused by infections especially viral, radiation, drugs (medications), chemicals, or toxins. |
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the yellowish staining of the skin and sclerae (the whites of the eyes) that is caused by high levels in the blood of bilirubin. |
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the death of living cells or tissues |
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Reticuloendothelial System (RES) |
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a group of living cells having the ability to take up and sequester inert particles and vital dyes. |
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Largest gland in the body composed of two main lobes, located in the mid to upper abdominal cavity |
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network of ducts that connect the liver, gallbladder, and duodenum |
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enzymes that have an active site and an additional (allosteric) sites to which small molecules, called effectors, can bind. |
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a form of negative allosterism that frequently orrucs in a series of enzyme reactions that constitute a metabolic pathway. |
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enzymes produces in a precursor inactive state. |
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chemical groups are covalently added or removed from the enzyme. |
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