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Biochemistry Flashcards

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14367396778Chiral amino acidsall but glycine0
14367397690S configuration amino acidsall but cysteine1
14367399513Nonpolar, non aromatic amino acidsglycine, leucine, arginine, alanine, methionine. lysine, valine, isoleucine, histidine, proline2
14367406242Positively charged amino acidsarginine, lysine, histidine3
14367407168Negatively charged amino acidsaspartic acid, glutamic acid4
14367408539Polar amino acidserine, threonine, cysteine, asparagine, glutamine5
14367411339Aromatic side chainstryptophan, phenylalanine, tyrosine6
14367523385Peptide bond formationcondensation/dehydration reaction with a nucleophilic amino group attacking an electrophilic carbonyl7
14367529079Peptide bond brokenby hydrolysis8
14367529947Primary structurelinear sequence of amino acids9
14367531713Secondary structurelocal structure, stabilized by hydrogen bonding (alpha-helices, beta sheets)10
14367535666Tertiary structurethree-dimensional structure stabilized by hydrophobic interactions, acid-base interactions (salt bridges), hydrogen bonding, and disulfide bonds11
14367541937Quaternary structureinteractions between subunits12
14367544256Enzymeslike 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
14367556410Ligasesresponsible for joining two large biomolecules, often of the same type14
14367556425Isomerasescatalyze the interconversion of isomers, including both constitutional and stereoisomers15
14367558973Lyasescatalyze cleavage without the addition of water and without the transfer of electrons. The reverse reaction (synthesis) is usually more biologically important.16
14367561684Hydrolasescatalyze cleavage with the addition of water17
14367562515Oxidoreductasescatalyze oxidation-reduction reactions that involve the transfer of electrons18
14367564461Transferases (kinases)move a functional group from one molecule to another molecule, catalyze the transfer of a phosphate group, generally from ATP, to another molecule19
14367600547Saturation KineticsAs substrate concentration increases, the reaction rate does as well until a maximum value is reached20
14367602809V= Vmax[S] / Km + [S]Michaelis-Menten equation21
14367605766At one half Vmax, [S] =Km22
14367607987competetive inhibitorbinds at active site, increases Km and no change on Vmax23
14367661263non-competitive inhibitorbinds at allosteric site, no change on Km, and decreases Vmax24
14367667279Mixed inhibitor25

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