enzymes

• substrate -reactant in an enzyme-catalyzed reactiom
• carbonic anhydrase -catalyze the removal of CO2 out of the body, which combines CO2 with water to form carbonic acid
• urease -catalyzed the hydrolysis of a single amide, urea
• enzyme specificity -extent to which an enzyme's activity is restricted to a specific substrate, a specific group of substrate, specific type of chemical bond, or a specific type of chemical reaction
• degree of specificity is determined by the active site
• absolute specificity -catalyze only one reaction and the most restrictive of all specificities (e.g., catalase)
• group specificity -act only on molecules that have a specific functional group, such as hydroxyl, amino, or phosphate group
• group specificity -carboxypeptidase is an example of this type of specificity
• linkage specificity -act on a particular type of bond irrespective to the rest of the molecular structure, and it is consider as the most general of the common species
• phosphatases -hydrolyzes phosphate ester bonds in all types of phosphate esters, and is an example of linkage specificity
• stereochemical specificity -act on a particular isomer, and catalyzes the reaction of only one of two possible enantiomers
• relative specificity -catalyzes the reaction of structurally related substance (e.g., lipases- hydrolyze lipids , proteases- split up proteins
• oxidoreductase (EC 1) -oxidation-reduction reactipn
• Transferases (EC 2) -catalyzes the transfer of functional groups
• transaminases -transfer of amino group
• kinases -transfer of phosphate group from ATP to give ADP
• Hydrolase (EC 3) -catalyzes hydrolysis reaction and it is central to the process of digestion (carbohydrases, proteases, and lipases)
• Lyase (EC 4) -addition of a group to a double bond or removal of a group from a double bond in a manner that does not involve hydrolysis or oxidation
• Isomerases (EC 5) - catalyze intramolecular rearrangement reactions
• isomerase (EC 5) -isomeration reaction
• Ligases (EC 6) -bonding together of two molecules into one with ATP cleavage
• enzyme active site -small part of an enzyme that is actually involved in catalysis
• enzyme active site -a three-dimensional entity formed by groups that came from parts of the protein chain
• enzyme-substrate complex -formed when a substrate binds to the active site of an enzyme
• phosphotases -formation of ester linkage
• decarboxylase -removal of carboxyl groups from compound
• peptidase -hydrolysis of peptide linkages
• esterase -hydrolysis of phosphate ester linkages
• lock and key model -Active site in the enzyme has the fixed, rigid geometrical conformation.
• lock and key model -Substrate with a complementary geometry can be accommodated.
• induced fit model -the enzyme’s active site is not rigid and static. There’s a constant change in shape
• induced fit theory -Allows for changes in the shape or geometry of the active site of an enzyme to accommodate a substrate. Result of the enzyme’s flexibility; it adapts the incoming substrate.
• simple enzyme -composed only of protein
• conjugated enzyme -has a non-protein part in addition to a protein part
• cofactor -non-protein part of conjugated enzyme
• apoenzyme -protein part of conjugated enzyme
• holoenzyme -cofactor together with apoenzyme
• cofactor -has two kinds; inorganic (metal ions), and organic
• organic -is tightly bound and called prosthetic group
• coenzyme -cofactor that is released free after reaction (e.g., NADH, NADPH)