Biochemistry Flashcards

6314746626	Primary structure	amino acid sequence	0
6314774911	hydrolase	hydrolyzes chemical bonds (Atlases, proteases)	1
6314777422	Isomerase	rearranges bond within a molecule to form an isomer	2
6314781498	Ligase	forms a chemical bond (DNA ligase)	3
6314783816	Lyase	break chemical bonds by means other than oxidation or hydrolysis (pyruvate decarboxylase)	4
6314790537	Kinase	transfer a phosphate group to a molecule to a molecule from a high energy carrier, such as ATP (phosphofructokinse PFK)	5
6314797698	Oxidoreductase	runs reduce reactions	6
6314801670	Polymerase	polymerization (addition of nucleotides to the leading strand of DNA by DNA polymerase)	7
6314804334	Phosphatase	removes a phosphate group from a molecule	8
6314817453	Protease	hydrolyzes peptide bonds	9
6314842582	Competitive inhibitors	-compete with substrate for the active site -Vmax is not changed -Km is increased, because you can overcome the inhibitor by increasing the amount of substrate - the affinity is decreased because it takes more substrate to reach Km -Think of it as a alcoholic versus freshman The alcoholic is going to take a lot longer to get drunk because his tolerance is increased (Km increased), thus his receptors are less sensitive, his affinity has decreased A freshman who doesn't drink, will only need a few beers to get drunk (Km) so the Km is decreased, thus the freshman has more affinity for the alcohol from one beer.	10
6314895703	Non competitive inhibitor	-Inhibitor can bind to the enzyme with or without the substrate bond to it -Vmax is decreased because the amount of functional ES complexes is decreased. -the substrate can bind without any problems, so Km does not change	11
6315017462	Uncompetitive inhibition	-Inhibitor binds the to allosteric site of the ES complex and does not allow the product to be made. -Reduces the number of functioning ES complexes, thus reduces product -Vmax is decreased -Km has decreased, the affinity has increased, the enzyme complex has such a high affinity for the substrate that it will not leave the active site of the enzyme complex On the plot,it is opposite of what you say since its the inverse.	12
6315255331	Line weaver-Burke Plot	slope: Km/Vmax y-intercept: 1/vmax x-intercept: -1/Km Increase in substrate concentration means a decrease in the value along the x-axis because it is the inverse increase the reaction rate V is a decrease in the inverse of the reaction , so reaction rate increases, the value along the y-axis decreases.	13
6315306695	Bronsted-Lowry Acids and bases	BAD Bronsted, Acid, Donates Acid: Protons (H+) donors Base: Proton (H+) accepters	14
6315330449	Oxidation Reaction Reduction Reaction	Oxidation: Gain of oxygen molecule, loss of hydrogen atoms, loss of electrons Reduction: is the opposite of oxidation	15
6315342432	Exergonic Endergonic	Negative Delta G Postive Delta G	16
6315342433	Ka value pka value	-the larger the Ka the stronger the acid; the smaller the Ka value, the weaker the acid -lower pka, stronger the acid, easily deprotonated -pH greater than pka, acid is deprontonated (basic solution)	17
6315393392	Secondary structure	Hydrogen bonds between back bond, Proline kinks for beta sheets, and alpha helix	18
6315398089	Tertiary structure	hydrophobic and hydrophilic interactions between amino acids residues located more distantly from each other in the polypeptide chains.	19
6315410854	Quaternary structure	various bonds between separate chains	20
6315575959	Vmax	Constant, it depends on enzyme concentration and what enzyme you have. Vmax is when all substrates are fully saturated, when enzymes are attached to active site all the time	21
6315601515	Km	How much substrate you need to have in order to make 1/2 vmax -measure of the enzymes affinity for that specific substrate -Km low, the enzyme has a high affinity for that substrate -Km high, the enzyme does not have a high affinity for that substrate (drink a lot, need more alcohol to get buzz)	22
6331065151	Periodic table trends		23