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20 Cards in this Set
- Front
- Back
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2 reasons reactants are more stable than ATP + H20
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1) resonance stabilization of Pi
2) electrostatic repulsion in ATP |
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4 highest energy storage molecules
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1) phosphoenolpyruvate (-14.8kcal/mol)<br />2) creatine phosphate (-11.8kcal/mol)<br />3) 1,3-bisphosphoglycerate (-10.3kcal/mol)<br />4) ATP (-7.3kcal/mol)
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when is creatine used to generate energy?
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after exercise--effective source of ATP for first 4 seconds only
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why do fatty acids have more energy than glucose?
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because fatty acids have carbons that are more reduced
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6 types of metabolic reactions
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1) redox reactions
2) ligation 3) isomerization 4) group transfer 5) hydrolytic 6) lyases (double<=>single bonds) |
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3 activated carriers
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NAD+ (nicotinamide adenine dinucleotide)
FAD (flavind adenine dinucleotide) Coenzyme A |
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reactive part of NAD+
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nicotinamide ring (pyridine derivative)
ring accepts H ion and 2 electrons |
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reactive part of FAD
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isoalloxazine ring--accepts 2 electrons and 2 protons
derived from vit B2 |
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coenzyme A
(what does it carry, what is reactive site, how much energy) |
carries acyl groups
change in E=-7.5 reactive site=terminal sulfhydral group in CoA |
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acyl groups are linked to CoA by what bonds
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high energy thioester bonds (resulting derivative is acyl CoA)
an acyl group commonly linked to CoA is acetyl |
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name the precursors of the following compounds:
FAD, FMN NAD CoA |
B2-riboflavin
niacin panthothenic acid |
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ligation reactions
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form bonds by using free energy from ATP cleavage
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isomerization reactions
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rearrange particular atoms within a molecule--role is often to prepare a molecule for subsequent reactions (i.e. redox)
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example of a group transfer reaction
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ATP
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hydrolytic reactions
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cleave bonds by the addition of H2O
break down large molecules |
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reactions involving the addition of functional groups to double bonds or removal of groups to form double bonds (+ example)
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enzymes catalyze reaction--lyases
i.e. fructose 1,6-bisphosphate to 3-C fragments |
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3 ways metabolic processes are regulated
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amount of enzyme--change rate of transcription of the genes encoding them
catalytic activities--reversible allosteric control, reversible covalent modification, energy status accessibility of substrates--compartmentalization segregates opposed reactions, flux of substrates |
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reversible allosteric control
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1st reaction in many biosynthetic pathways is allosterically inhibited by product
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energy charge
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index of energy status in cell
E.C.=([ATP]+1/2[ADP])/([ATP]+[ADP]+[AMP]) most cells have EC of 0.8 to 0.95 |
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when energy charge=0,...
when energy charge=1,... |
=0, [AMP] dominates, ATP generating pathway is favored
=1, [ATP] dominates, ATP utilization favored |
