14367396778 | Chiral amino acids | all but glycine | 0 | |
14367397690 | S configuration amino acids | all but cysteine | 1 | |
14367399513 | Nonpolar, non aromatic amino acids | glycine, leucine, arginine, alanine, methionine. lysine, valine, isoleucine, histidine, proline | 2 | |
14367406242 | Positively charged amino acids | arginine, lysine, histidine | 3 | |
14367407168 | Negatively charged amino acids | aspartic acid, glutamic acid | 4 | |
14367408539 | Polar amino acid | serine, threonine, cysteine, asparagine, glutamine | 5 | |
14367411339 | Aromatic side chains | tryptophan, phenylalanine, tyrosine | 6 | |
14367523385 | Peptide bond formation | condensation/dehydration reaction with a nucleophilic amino group attacking an electrophilic carbonyl | 7 | |
14367529079 | Peptide bond broken | by hydrolysis | 8 | |
14367529947 | Primary structure | linear sequence of amino acids | 9 | |
14367531713 | Secondary structure | local structure, stabilized by hydrogen bonding (alpha-helices, beta sheets) | 10 | |
14367535666 | Tertiary structure | three-dimensional structure stabilized by hydrophobic interactions, acid-base interactions (salt bridges), hydrogen bonding, and disulfide bonds | 11 | |
14367541937 | Quaternary structure | interactions between subunits | 12 | |
14367544256 | Enzymes | like all catalysts, lower the activation energy necessary for reactions. They do not alter free energy (delta G) or enthalpy (delta H) change that accompanies the reaction nor the final equilibrium position; rather, they change the rate (kinetics) at which equilibrium is reached. | 13 | |
14367556410 | Ligases | responsible for joining two large biomolecules, often of the same type | 14 | |
14367556425 | Isomerases | catalyze the interconversion of isomers, including both constitutional and stereoisomers | 15 | |
14367558973 | Lyases | catalyze cleavage without the addition of water and without the transfer of electrons. The reverse reaction (synthesis) is usually more biologically important. | 16 | |
14367561684 | Hydrolases | catalyze cleavage with the addition of water | 17 | |
14367562515 | Oxidoreductases | catalyze oxidation-reduction reactions that involve the transfer of electrons | 18 | |
14367564461 | Transferases (kinases) | move a functional group from one molecule to another molecule, catalyze the transfer of a phosphate group, generally from ATP, to another molecule | 19 | |
14367600547 | Saturation Kinetics | As substrate concentration increases, the reaction rate does as well until a maximum value is reached | 20 | |
14367602809 | V= Vmax[S] / Km + [S] | Michaelis-Menten equation | 21 | |
14367605766 | At one half Vmax, [S] = | Km | 22 | |
14367607987 | competetive inhibitor | binds at active site, increases Km and no change on Vmax | 23 | |
14367661263 | non-competitive inhibitor | binds at allosteric site, no change on Km, and decreases Vmax | 24 | |
14367667279 | Mixed inhibitor | 25 |
Biochemistry Flashcards
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