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Microbiology
Vocabulary chapter 5,6 &7
| Question | Answer |
|---|---|
| Enzymes | large globular proteins, names that end in ---ase, regulate complex biochemical reactions by reducing activation energy, substrate, active site, specificity |
| substrates | As catalysts, each enzyme acts on a specific substance, called the enzyme's substrate |
| products | |
| adenosine triphosphate (ATP) | |
| catabolic | reactions couple with ATP synthesis |
| anabolic | reactions couple with ATP breakdown |
| catabolism | in living cells, the enzyme -regulated chemical reactions that release energy / provides energy and building block for anabolism |
| anabolism | mostly involved enzyme-regulated energy-requiring reactions / uses energy and building blocks to build large molecules |
| metabolism | the sum of the chemical reaction within a living organism |
| metabolic pathway | is a sequence of enzymatically catalyzed chemical reactions in a cell |
| nitrogen cycle | key component in proteins, DNA, RNA and plant chlorophyll |
| collision theory | states that chemical reactions can occur when atoms, ions, and molecules collide the energy transferred by the particles in the collision can disrupt their electron structures enough to break chemical bonds or form new bonds |
| activation energy | is needed to disrupt electronic configurations, the amount of energy needed to disrupt the stable electronic configuration of any specific molecule so that the electrons can be rearranged |
| reaction rate | the frequency of collisions with enough energy to bring about a reaction |
| turnover number | the maximum number of substrate molecules an enzyme converts to product each second, generally 1 to 10000 and can be as high as 500,000 |
| enzyme-substrate complex | a temporary union of an enzyme and its substrate |
| apoenzyme | the protein portion of an enzyme, which requires activation by coenzyme |
| cofactor | the nonprotein component of an enzyme, a microorganism or molecule that acts with other to synergistically enhance or cause disease |
| coenzyme | a non protein substance that is associated with and that activated an enzyme |
| holoenzyme | an enzyme consisting of an apoenzyme and a cofactor |
| oxidoreductase | oxidation-reduction, in which oxygen and hydrogen are gained or lost examples; cytochrome oxidase, lactate dehydrogenase |
| transferase | transfer of functional groups, such as an amino group, acetyl group, or phosphate group example; acetate kinase, alanine deaminase |
| hydrolase | hydrolysis (addition of water) example; lipase and sucrase |
| lyase | removal of groups of atoms without hydrolysis example; oxalate decarboxylase, isocitrate lyase |
| isomerase | rearrangement of atoms within a molecule example; glucose-phosphate isomerase, alanine racemase |
| ligase | joining of two molecules (using energy usually derived from the breakdown of ATP) examples; acetyl-CoA synthetase, DNA ligase |
| nicotinamide adenine dinucleotide (NAD+) | a coenzyme that functions in the removal and transfer of hydrogen ion (H-) and electrons from substrate molecules |
| NADP+ | a coenzyme similar to NAD+ |
| flavin adenine dinucleotide (FAD) | flavin adenine dinucleotide; a coenzyme that functions in the removal and transfer of hydrogen ions (H1) and electrons from substrate molecules |
| flavin mononucleotide (FMN) | flavin mononucleotide; a coenzyme that functions in the transfer of electrons in the electron transport chain |
| Coenzyme A(CoA) | a coenzyme that functions in decarboxylation |
| denaturation | a change in the molecular structure of a protein, usually making it nonfunctional |
| denaturation of a protein | breaking of noncovalent bonds (such as hydrogen bonds) that hold the active protein in its three dimensional shape renders the denatured protein nonfunctional |
| saturation | the condition in which the active site on an enzyme is occupied by the substrate or product at all times. In a fatty acid, having no double bonds |
| competitive inhibitor | a chemical that competes with normal substrate for the active site of an enzyme. |
| enzyme inhibitors | an uninhibited enzyme and its normal substrate, a competitive inhibitor, one type of noncompetitive inhibitor, causing allosteric inhibition |
| noncompetitive inhibitor | an inhibitory chemical that does not compete with the substrate for an enzyme's active site. |
| allosteric inhibition | the process in which an enzyme's activity is changed because of binding to the allosteric site. |
| allosteric site | the site on an enzyme at which a noncompetitive inhibitor binds |
| feedback inhibition or end-product inhibition | inhibition of an enzyme in a particular pathway by the accumulation of the end-product of the pathway; also called end-product inhibition |
| ribozyme | an enzyme consisting of RNA that specifically acts on strands of RNA to remove introns and splice together the remaining exons |
| oxidation | the removal of electrons from a molecule |
| reduction | the addition of electrons to a molecule |
| oxidation-reduction | a coupled reaction in which one substance is oxidized and one is reduced; also called redox reaction |
| stopped at page 118 |
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sillylilia
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