Chapter 5 Set 1

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jamnurse Plus on June 8, 2012

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Chapter 5 Set 1

metabolism
___ is the sum of all chemical reactions; a balancing act between acquiring & using energy; 2 types: catabolic & metabolic.
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metabolism ___ is the sum of all chemical reactions; a balancing act between acquiring & using energy; 2 types: catabolic & metabolic.
catabolic ___ metabolism breaks bonds & releases energy from more complex molecules (exergonic), and are generally hydrolytic reactions.
exergonic ___ is accompanied by the release of energy.
catabolic, anabolic ___ reactions provide the building blocks for, and generate the energy / ATP to drive, ___ reactions.
catabolizes ATP ___ and forms ADP + P + energy released as heat
anabolic ___ metabolism forms bonds & requires energy to build more complex molecules (endogonic), and are generally dehydration synthesis reactions.
anabolizes ADP + P + energy ___ and forms ATP.
coupled all metabolic reactions are ___.
coupled ___ is a reactions that occurs back to back.
made, spent energy is ___ then ___.
ATP, energy glucose breaks down into ___, which immediately breaks down into ADP + P, which is the ___ we use.
proteins ___ are broken down into amino acids.
carbohydrates ___ are broken down into starches & sugars.
fatty acids, trigyceride true fats are 3 ___ ___ + 1 ___.
enzymes in living cells ___ are always the catalysts of reactions.
proteins enzymes are large globular ___, with the exception of lysozymes & ribozymes.
substrate enzymes are always ___ specific (lock & key).
accelerate enzymes usually ___ a reaction.
substrate, lowers, temperature enzymes act by properly orienting a ___ to its active site, which ___ the activation energy, so a reaction can accelerate without increasing the ___.
enzyme the nomenclature "ase" or "yme", means ___.
remove the nomenclature "de" means ___.
dehydrogenase ___ is an enzyme that removes hydrogen.
decarboxylase ___ removes COOH or COO-.
apoenzyme, coenzyme, holoenzyme an ___ & a ___ form a complete active enzyme called a ___.
apoenzyme an ___ is the protein portion of a holoenzyme, and is inactive on its own.
coenzyme a ___ is the nonprotein or organic molecule that either accepts, donates or carries an electron portion of a holoenzyme .
NAD+, NADP+, FMN, FAD important coenzyme electron carriers, from most to least: ___, ___, ___ & ___.
coenzyme A ___ ___ is involved in the synthesis of fats, as well as a series of oxidizing reactions in the krebs cycle.
3,4,2,1 put the following steps of an enzymatic action in order:
1. products are released (enzyme is unchanged).
2. substrate is changed into a specific product.
3. substrate binds to the active site.
4. forms an enzyme substrate complex (lowers energy of activation).
temperature, pH, substrate concentration, inhibitors factors that influence enzymatic activity are ___, ___, ___ ___ & ___.
temperature the higher the ___, the faster the reaction.
bacteria for most disease causing ___ the optimal temperature is body temperature (35-40 C).
denature, catalyze temperatures above or below 35-40 C causes the proteins in a disease causing bacteria to ___, which causes the active site to change & the enzyme can no longer ___ the reaction.
denature both acid pH & basic pH can ___ an enzyme.
saturation, increase under high substrate concentration, the enzyme is in ___, so further ___ in concentration will not affect the reaction rate.
saturated, inactive, concentration under normal cellular conditions, enzymes are not ___ with substrate, so many molecules are ___, & ___ is likely to influence rate of reaction.
inhibitors ___ control bacteria by controlling their enzymes.
competitive ___ inhibitors have a similar shape & chemical structure to substrate, and compete to fill the active site of an enzyme.
substrate increasing the amount of ___ might overcome a competitive inhibitor.
denatured if the AA sequence is as programmed, it will fold properly, but if the sequence is wrong, shape changes & the protein will become ___.
feedback inhibition ___ ___ occurs if there is enough substrate at the end of an enzymatic action to allosterically bind to the initial reactant, & shut down the pathway.

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