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36 Cards in this Set
- Front
- Back
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What are the enzymes used to convert a protein to amino acids?
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Pepsin --> gets to polypeptides
Chemotrypsin and trypsin --> convert to AA |
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What are the stages in protein metabolism?
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1.) Transamination
2.) Oxidative deamination |
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All amino acids transfer the Amines to what molecule in protein metabolism?
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Alpha ketogluterate! Converts this to the amino acid glutamate!
(this is just a transfer of the NH3 for the ketone) (part of oxidative deamination) |
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What does the alpha ketogluterate swap in transamination?
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It swaps its ketone for the NH3 on the amino acid.
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Where does the ketone part from the original alpha ketoglutarate go in transamination?
What kind of molecule does this make? |
It is swapped with the amine of an amino acid. This makes a keto acid! (such as pyruvate, if alanine is the AA used) (pg 857)
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If alanine is the amino acid involved in transamination, what does it get converted to?
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Pyruvate
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What does the alpha ketogluterate get converted to in transamination?
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Glutamate
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After glutamate is created by the process transamination, what can happen to the product glutamate.
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It can add another NH3, creating glutamine. Or it can remove the added NH3 by the process of oxidative deamination and reform alpha ketogluterate and Ammonia for the Urea cycle! (pg 857)
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Which molecule can lose a -NH3 piece in the protein metabolism pathway called oxidative deamination, Glutamine or Glutamate?
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Glutamate
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The conversion of Glutamate back to Alpha ketogluterate is what kind of reaction?
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oxidative deamination
(requires NADH and H2O) (Glutamate dehydrogenase is the enzyme doing this) |
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What enzyme would be require to remove the NH3 from the amino acid Alanine and have it placed on Glutamate in transamination of an amino acid?
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Alanine transaminase
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What is the end result of the amino acid in transamination?
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THe amine (-NH3) is removed and a ketone is added in its place.
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What electron carrier is used to do oxidative deamination to return glutamate back to alpha ketogluterate?
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NAD+ or NADP+
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What does the process of oxidative deamination in protein metabolism produce?
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Ammonia (NH4+) to go to the urea cycle (Also produces NADH or NADPH)
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If alanine is the protein that undergoes protein metabolism, what carbon molecule will it make after transamination?
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pyruvate (glucogenic AA)
(amino acids that can be used to make glucose) |
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If you entered the citric acid cycle at Alpha ketogluterate how many ATP would you get?
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9 ATP (because it produces 1 less NADH... which equals 3 atp lost)
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If you entered the citric cycle at oxaloacetate how many ATP would you get?
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12 ATP
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Ammonia added to CO2 makes what kind of molecule?
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carbamoyl phosphate
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The making of carbamoyl phosphate requires what reagents?
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CO2, Ammonia, 2 ATP (spits out 2ADP + Pi)
(Enzyme needed is carbamoyl phsphate synthethase) |
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What does carbamoyl phosphate combine with?
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Ornithine
A 5 carbon and 2 Nitrogen compound |
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Eventually how many carbons and nitrogens are condensed in the urea cycle?
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10 Carbons / 4 nitrogens
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What is the end product of the urea cycle?
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Urea! 1 Carbon, 2 Nitrogens
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What happens to arginine in the urea cycle?
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On the side chain the Carbon double bonded to NH2 and single bonded to NH2 is cleaved from the sidechain to make urea
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When carbamoyl phosphate combines with ornithine, what molecule is created?
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Citrulline
(Phosphate on carbamoyl phosphate condense with the NH3 on side chain) H and Phosphate are lost |
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Where does the urea cycle start?
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In the matrix
(goes into the cytosol after it creates citrulline) |
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After which molecule is made, is the urea cycle takin place in the cytosol?
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After it creates citrulline it can cross into the cytosol
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In the urea cycle, what does citrulline combine with after it crosses in the cytosol? WHat does it create?
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- aspartate
- arginino succinate |
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How does the arginino succinate get fromed from the original citrulline after it combines with aspartate?
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The O that is double bonded is lost and the double bound is now attached to the Nitrogen in the amine of Aspartate. (the connecting bond is a N double bonded to the original molecule citrulline
(this is hard to explain but make sure you know based on the picture on pg 859) |
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What is the enzyme called that combines the citrulline and aspartate?
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Argininosuccinate Synthetase!
(requires ATP - which goes to AMP!! Spits out 2 inorganic phosphates because they are not used) |
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In the urea cycle, after argininosuccinate is created, what molecule does it transform to?
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Fumerate
(Takes almost all of the recently aspartate in the previous step, but leaves the Nitrogen on the big molecule) |
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Which enzyme comes first in the urea cycle argininosuccinase or argininosuccinate synthetase?
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argininosuccinate synthetase
(This combines the citrulline with aspartic acid) (argininosuccinase makes fumerase) |
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( get a question for after fumarate is formed)
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YEs do it!
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In the urea cycle, the extra nitrogen comes from which molecule?
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Aspartate
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The splitting off of urea from arginine require which enzyme and what type of class of enzyme is this enzyme?
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Requires arginase (which uses water) Which makes it a hydrolase
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In the urea cycle, converting citrulline to argininosuccinate is done by which enzyme? What kind of enzyme class is this?
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argininiosuccinate synthetase (which uses ATP) So that is a ligase enzyme
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In the urea cycle, converting argininosuccinate to arginine is done by which enzyme?
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Argininosuccinase, which is a lyase enzyme
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