4589812
Beschreibung
Karteikarten von Samantha Scruggs, aktualisiert more than 1 year ago
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Erstellt von Samantha Scruggs
vor fast 9 Jahre
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| Frage | Antworten |
| 6 different types of enzymes | 1. oxidoreductases 2. hydrolases 3. isomerases 4. transferases 5. lyases 6. ligases |
| isozymes | different structural forms of a protein that catalyze the same reaction. |
| oxidoreductases | catalyze oxidation-reduction reactions. Examples - dehydrogenases, oxidases, reductases, peroxidases, catalase, oxygenases, hydroxylases Electrons are removed from one substrate and added to another. |
| transferases | transfer a chemical group from one molecule to another. Examples - transaldolase, transketolase, acyl, methyl, glucosyl and phosphoryltransferases, kinases, phosphomutases For example, aminotransferases transfer the amino group to convert an AA to a ketoacid. They require Vitamin B6 |
| hydrolases | catalyze hydrolysis reactions. examples: esterases, glycosidases, peptidases, phosphatases, thiolases, phospholipases, amidases, deaminases, ribonucleases transfer -OH from water to substrate. Irreversible reaction. Substrate is typically an ester or an amide. |
| lyases | break apart a bond, usually a carbon-carbon bond. Can also be carbon-nitrogen, or release CO2 from a B-keto-acid. Examples - decarboyxlase, aldolases, hydratases, dehydratases, synthases, lyases if ATP is required, it's called synthetase. If not, it's synthase. |
| isomerases | Involved with moving a group or a double bond within the same molecule. Examples: racemases, epimerases, isomerases, mutases (not all) Mutase is when a phosphate is moved from one carbon to another within the same molecule such as occurs with phosphglycerate mutase that converts 2-phosphoglycerate to 3-phosphoglycerate |
| ligases | join carbon atoms together, but unlike lyases, they require energy for the reaction and are referred to as synthetases. Also carboxylases. Energy usually comes from ATP. |
| binding of a substrate by an enzyme | for an enzyme to function as a catalyst (which increases the rate of the reaction, but does not change equilibrium or K), it must first bind the substrate and then lower the energy of activation so that the reaction will proceed at a faster rate than it would in the absence of the catalyst. Two prevalent theories exist to explain how substrates bind the enzyme - lock and key theory, and induced-fit theory |
| lock and key theory | proposes that a binding site for substrate on the enzyme is a rigid entity and only a compound with a particular shape will fit, analogous to how a lock allows only one key to make the proper contact. |
| induced-fit theory | Assumes that the enzyme is flexible, and after the substrate binds the enzyme, the conformation of the protein changes so that a stable binary complex forms. |
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