LSCI 211 Lecture Notes - Lecture 9: Dna Ligase, Non-Covalent Interactions, Isomerase
28 Aug 2016
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Document Summary
Proteins that increase the rate of a reaction in physiological conditions. Catalyze reactions in both directions; both forwards and backwards. Enzymes can be part of one or more of the following groups. Transferases- transfers of groups (acetyl, methyl, phosphate etc) Lyases- addition of groups across a double bond or elimination of groups to create a double bond. Ligases- joining of two molecules using energy from atp. Some enzymes function as monomers, some require quaternary structure. Many proteins require non-protein cofactors to complete the active site on the enzyme. May bind to the apoenzyme by non-covalent bond to make a holoenzyme. May interact via a covalent bond and not disassociate even after denaturation. Inorganic- metal ions na+, k+, mg2+, mn2+, zn2+, co2+, mo6+, fe2+, and fe3+ Organic (coenzymes)- vitamins: ascorbic acid (c), folic acid, thiamine (b12), k. Orient reactants in the reactive conformation in the active site. They do not alter the chemistry of a reaction, or get consumed.
