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38 Cards in this Set
- Front
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define amphipathic |
part polar, part non polar. Used to refer to the hydrophobicity of lipids |
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Omega N fatty acids |
A way to count double bonds from the end of the tail. The location of that bond is denoted by omega |
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Define acylglycerol |
fatty acids esterified with glycerol are better for storage because they are almost entirely non polar. Therefore, you can fit them close tog |
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phospholipids |
Main material of membranes. Often saturated at position 1 and unsaturated at position 2. Could be 2 saturated but RARELY two unsaturated. Nature doesn't work that way |
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define genomics |
study of whole genome of organism |
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transciprtomics |
study of transcribed genome |
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proteomics |
study of protein expression and their modifications |
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metabolomics |
study of all metabolites (no estimate of possible number) |
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systems biology |
integration of data to develop predictive models |
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synthetis biology/biochemical engineering |
it is: the design and construction of new biological parts, devices and systems, and the re-design of existing, natural biological systems for useful purposes. (e.g. bacteria used to produce biofuel from glucose |
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autotrophs |
just use CO2 as carbon source |
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heterotrophs |
use organic forms of carbon |
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phototrophs |
use light as energy source |
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chemotrophs |
use organic chemicals as energy and in some case oxidisable inorganics |
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metabolons |
multienzyme complexes (common). metabolites are passed from one active site to another without complete equilibration with the bulk cellular fluids. this decreases intermediate transit time and prevents intermediate loss (diffusion, competing pathways) |
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catabolic pathways converge to a few products. this differs from anabolic pathways because |
anabolic pathways diverge to synthesize many biomolecules. amphobolic intermediates have roles in catabolism and anabolism |
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independent catabolism and anabolic pathways |
activation of one mode is accompanied by reciprocal inhibition of the other mode. For example, if enzyme 1 is turned on in the catabolic pathway (taking substrate A to create product P), enzyme 6 - which begins the anabolic pathway from P to A - gets turned off. Cell decides which to activate based on energy levels available to the cell |
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micronutrients |
are required in diet, not synthesized by the organism. Are components or precursors of coenzymes (except vitamin c). they may be carriers of specific functional groups |
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coenzyme |
required for certain enzymes to function. they are typically modified and then converted back by other enzymes. |
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NAD+ and NADP+ |
two-electron carrier coenzymes. transfer hydride anion (H- - 2 electrons) to and from substrates in redox reactions (usually dehydrogenase) |
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riboflavin and the flavins (vitamin B12) |
micronutrient. helps convert carbohydrates (glucose) into energy. The active forms are flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD). Can carry 0 1 or 2 electrons. |
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thiamine (vitamin B1) |
thiamine pyrophosphate (TPP) is the active form. it is involved in carbohydrate metabolism |
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vitamin B6: pyridoxine and pyridoxal phosphate |
catalyzes rxns involving amino acids. Can form stable Schiff base adducts with alpha-amino acid groups - this allows the electron to move in a conjugated electron sink system & this is stabilizing for the intermediate of the rxn |
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how does a schiff base work? |
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coenzyme A (vitamin b5 - panthothenic acid is a component of this) |
Serves two main functions: 1. activates acyl groups (Acyl refers to any group with thestructure R-(C=O) for transfer by nucleophilic attack, and 2. activation of the alpha-hydrogen of the acyl group to be abstracted as a proton. The reactive -SH group on CoA helps the reaction proceed (thioester bond) - makes it easier to grab something and release - does so with less energy |
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What does the panthothenic acid help with? Adenine nucleotide? |
This acts as an arm to grab the substrate and move it to a different activation site on the enzyme.
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biotin |
a micronutrient. functions as a mobile carboxyl group (-COOH) carrier. Binds to lysine - when this occurs its called biocytin. The "tether" allows biotin to acquire a carboxyl group at one subsite of enzyme then deliver it to a substrate acceptor at another enzyme subsite |
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lipoic acid (info) |
also a ring on a chain and gets linked to protein. This is an acyl group carrier, couples that transfer with an electron transfer during oxidation and decarboxylation of alpha-keto acids. This cofactor is used by pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase |
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lipoic acid (picture) |
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vitamin B12: cyanocobalam |
Catalyzes: 1. intramolecular rearrangements. 2. reductions of ribonucleotides to deoxyribonucleotides 3. methyl group transfers (using tetrahydrofolate - see folic acid) |
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folate |
Acceptors/donars of 1-C units for all oxidation levels of carbon except for CO2. Active form is THF (formed by 2 reductions of folate by duhydrofolate reductase) |
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vitamin c |
reducing agent, electron scavenger. It helps to hydroxylate proline and lysine, metabolizes Tyr and Fe in the spleen. Prevents toxicity of metals, reduces allergic responses, and stimulates the immune system |
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vitamin A |
important in development, cell differentiation. This is a prohormone, retinol from retinoic acid. |
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vitamin D |
prohormone. produced in skin in response to sunlight. is a ligand for vitamin D receptor. this is important in bone maintenance and calciummetabolism |
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which coenzymes are electron carriers? |
NADH, NADPH, FADH, FADH2 (vitamin C) |
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which coenzymes are involved in (de)carboxylation reactions? |
thiamine, vitamin B6, biotin |
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which coenzymes are involved in acyl group transfers? |
coA,lipoic acid (folic acid,vitamin B12) |
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which coenzymes use a tethering mechanism? |
coA, biotin, lipoic acid |