Term
| What are the 5 substrates of Pyruvate DH complex |
|
Definition
| TPP, Lipoate, CoA, FAD, NAD |
|
|
Term
| What are PDH parts and prosthetic groups? |
|
Definition
E1-TPP
E2-Lipoate
E3-CoA, FAD, NAD |
|
|
Term
| What is the fate of glycerol? |
|
Definition
| converted into glycerol-phosphate, than DHAP to G3P |
|
|
Term
| What are the domains of E2 in PDH complex? |
|
Definition
| Binding, acyltransferase, lipoyl |
|
|
Term
| What part channels the substrate in PDH |
|
Definition
|
|
Term
|
Definition
| decarboxylates pyruvate, TPP |
|
|
Term
|
Definition
| decarboxylates pyruvate, TPP |
|
|
Term
|
Definition
(Dihydrolipoyl transacetylase) Lipoate
and CoA as coenzyme,forms an
acetyl thioester and transfers the acyl group to CoA. |
|
|
Term
|
Definition
| (Dihydroxylipoyl dehydrogenase), with FAD and NAD+ as cofactor, regenerates the oxidized lipoyl group |
|
|
Term
| Why is Thiamine important? |
|
Definition
| lack of causes no PDH and therefore more lactate, brain uses PDH for most energy production |
|
|
Term
| What is an anaplerotic pathway? |
|
Definition
| pathway which regenerates the intermediates for CAC |
|
|
Term
| Where do the carbons come from after the first CAC turn? |
|
Definition
| not acetate from acetyl-CoA, comes from the old OAA |
|
|
Term
| What does cholecystokinin signal? |
|
Definition
| fat in stomach, releases bile salts for emulsification also release of proteolytic enzymes |
|
|
Term
| What does Pancreatic lipase do? |
|
Definition
| partially emulsifies TAGs into DAGs, and MAGs. |
|
|
Term
| Lipo proteins as packaged into what for transportation? |
|
Definition
|
|
Term
| What does Apolipoproteins do? |
|
Definition
| activate lipase which turn chylomicrons into fatty acids |
|
|
Term
| What protein blocks the lipase from attacking stored TAGs? |
|
Definition
|
|
Term
| How does Glucagon and epinephrine allow lipases to attack stored TAGs? |
|
Definition
| the activate the cAMP pathway which leads to phosphorylation of perilipin. |
|
|
Term
| What enzymes convert FFA to acyl-CoA? |
|
Definition
| fatty acyl-CoA synthetases |
|
|
Term
| What are the three end points of Fatty acyl-Coa? |
|
Definition
| membrane lipids, TAGs and oxidation in mito. |
|
|
Term
| What are the steps/pathway needed to transport FA into mito? |
|
Definition
| Carnitine Shuttle. FFA-acylCoA which is converted to a Carnitine ester by carnitine-acyltransferase I. Then converted back once inside. |
|
|
Term
| What blocks carnitine-acyl CoA? |
|
Definition
| Malonyl-CoA (first step in synthesis.) |
|
|
Term
| What are the 3 stages of FA oxidation? |
|
Definition
1.) Beta-oxidation
2.) acetyl groups go through CAC
3.) oxidative phosphorylation |
|
|
Term
| How many steps are in Beta-oxidation? |
|
Definition
| 4 steps, breaking bound at the beta carbon. by converting the Beta carbon into a ketone it is attacked |
|
|
Term
| What are the 4 enzymes in Beta-oxidation? |
|
Definition
Acyl-CoA dehydrogenases,
Enoyl-CoA hydratase, L-β-hydroxyacyl-CoA dehydrogenase, and thiolase |
|
|
Term
|
Definition
| trifunctional protein channels the end of Beta-oxidation and is attached to the inner mito membrane |
|
|
Term
| Which enzymes are the alpha and beta parts of TFP? |
|
Definition
alpha- enoyl-CoA
hydratase and β-hydroxyacyl-CoA
dehydrogenase
beta- thiolase |
|
|
Term
| What are the end products of each pass in Beta-oxidation? |
|
Definition
| 4 ATP, 1 molecule of H2O, and one acetyl-CoA. |
|
|
Term
| What enzyme corrects unsaturated FAs? |
|
Definition
|
|
Term
| what three enzymes convert propionyl-CoA to succinyl CoA? |
|
Definition
| propionyl-CoA carboxylase and Methylmalonyl-CoA epimerase Methylmalonyl-CoA mutase |
|
|
Term
| what is pernicious anemia. |
|
Definition
| lack of B12, cant metabolize odd number FAs |
|
|
Term
| What is unique about B12 reactions? |
|
Definition
| add the adenosine allowing the three Phosphates to fall off. |
|
|
Term
| what does acetyl-CoA carboxylase contain? |
|
Definition
| 3 parts: biotin carboxylase, biotin carrier protein and transcarboxylase |
|
|
Term
| how many domains does Fatty acid synthase type I? |
|
Definition
| two. create to FA at the same time. |
|
|
Term
| what four steps are repeated to add acetyl-Coa to FA? |
|
Definition
| attack of main chain, reduction, dehydration, reduction |
|
|
Term
| Fatty acid synthase type I is stopped by what? |
|
Definition
| thioesterase, after 7 cycles 16 carbons added |
|
|
Term
| Differences between ACP and CoA |
|
Definition
| ACP long bound protein has 4′-phosphopantetheine prosthetic group , CoA small soluble protein |
|
|
Term
| What does FA synthesis occur in plants/animals? |
|
Definition
|
|
Term
| Where does FA oxidation occur? plants and animals |
|
Definition
|
|
Term
| What is needed to add 2 carbons to a FA chain? |
|
Definition
| 1 ATP and 2 NADPH + 2 H+ before transportation 3 ATP + 2 NADPH + 2 H after getting it out of mito |
|
|
Term
| Can mammals produce unsaturated FA? |
|
Definition
| yes only C-16 and C-18 at carbon 9. cant between 10 and methyl though. |
|
|
Term
| How does Citrate regulate FA? |
|
Definition
| activates acteyl-CoA carboxylase producing malonyl-CoA |
|
|
Term
| What does Palmitoyl-CoA regulate FA? |
|
Definition
| inhibites acteyl-coa carboxylase halting FA synthesis |
|
|
Term
| what is the regulation of Acyl-coa carboxylase by hormones? |
|
Definition
| Glucagon and epinephrine trigger phosphorylation and inhibition of acetyl-CoA carboxylase insulin does reverse |
|
|
Term
| how are the enzymes in Beta-oxidation regulated? |
|
Definition
high [NADH]/[NAD+] inhibits β-hydroxyacyl-CoA
DH and high [acetyl-CoA] inhibits thiolase |
|
|
Term
| AMP-dependent kinase (AMPK) which does what? |
|
Definition
| phosphorylates and inhibits ACC |
|
|
Term
| What are two long term regulations of FA metablosim? |
|
Definition
| Glucagon, through the transcription factor CREB and PPAR (Peroxisome Proliferator-Activated Receptors), |
|
|
Term
| What does PPAR (Peroxisome Proliferator-Activated Receptors do? |
|
Definition
| stimulates production of oxidizing enzymes |
|
|
Term
| What is the difference between mito and pexosome/glyoxysome oxidation? |
|
Definition
| p and G pass electrons straight to O2, in H2O2. has high concentration of catalase need to export NADH and acetyl-coa to mito |
|
|
Term
| where does omega-oxidation occur? |
|
Definition
|
|
Term
| What is unique bout omega-oxidation? |
|
Definition
| gives off succinate (carb from FA) and oxidation from both ends |
|
|
Term
| What is alpha oxidation used for? |
|
Definition
|
|
Term
| alpha-oxidation leads to carbs how? |
|
Definition
| breaks off a propionyl acid and that leads to succinyl-CoA |
|
|
Term
| what are the reasons for using ketone bodies? |
|
Definition
| free up CoA in liver and to transport energy to muscles/brain |
|
|
Term
| What are three ketone bodies? |
|
Definition
| acetone, acetoactone and beta-hydroxyburyrate |
|
|
Term
| What is acidosis caused by? |
|
Definition
| decrease in pH by accumulation of ketone bodies |
|
|
Term
| where are ketone bodies formed? |
|
Definition
in the matrix of liver
mitochondria |
|
|
Term
| how many CoA are produced per ketone body? |
|
Definition
|
|
Term
| what enzyme does the liver lack which stops ketone metabolism? |
|
Definition
β-ketoacyl-CoA transferase,also called
thiophorase, |
|
|
Term
| each Beta-hydroxybutyrate produces what when converted back? |
|
Definition
|
|
Term
| Why is HMG-lyase stored in the mito? |
|
Definition
| so it can not interfere with cholesterol synthesis |
|
|
Term
| What are the two main sites of protein degradation ? |
|
Definition
|
|
Term
| What kind of proteases are present in lysosome? |
|
Definition
many cysteine proteases, as well as some
aspartate proteases and one zinc protease |
|
|
Term
| What kind of proteases are present in proteasome? |
|
Definition
|
|
Term
| what hormone is used to release HCl and histamine? |
|
Definition
|
|
Term
| Chief cells secrete what? |
|
Definition
| pepsinogen, which auto cleaves and attacks protein |
|
|
Term
| What does secretin do in the small intestines? |
|
Definition
| causes the release of bicarbonate which neutralizes the acid |
|
|
Term
| What converts trypsinogen to trypsin? |
|
Definition
| enterpeptidase from the pancreas which si protected by pancreatic trypsin inhibitor |
|
|
Term
| what three forms can ammonia by transferred to liver as? |
|
Definition
| alanine. glutamine, glutamate |
|
|
Term
| What is the process of transamination? |
|
Definition
transfer of Nitrogen to ketoglutaric
acid, ends in glutamate specific to donor. |
|
|
Term
| What is the prosthetic group for transamination? |
|
Definition
|
|
Term
| What is the process of deamination? |
|
Definition
| Glutamate Dehydrogenase acts on glutamate converting to ketoglutarate and releasing NH4, in mitochondria |
|
|
Term
| What do tissues use to convert NH4 into glutamine? |
|
Definition
|
|
Term
| What enzyme does the liver use to convert back to glutamate? and NH4 |
|
Definition
|
|
Term
| What is the positive reason to use alanine for a NH4 transporter? |
|
Definition
| removes extra pyruvate from muscles |
|
|
Term
| What happens in the glucose-alanine cycle? |
|
Definition
| glucose is shipped to muscles after alanine is broken down in liver to NH4 and pyruvate |
|
|
Term
| what are the three forms of nitrogen excretion ? |
|
Definition
| ammonia, urea, and uric acid |
|
|
Term
| Where do the two amino groups enter the urea cycle? |
|
Definition
mito (ammonia (carbamoyl
phosphate)) and cytosol as aspartate |
|
|
Term
| What does carbamoyl phosphate synthetase I do? |
|
Definition
| produce carbamoyl phosphate, by combination of 2 ATP and 1 NH3 |
|
|
Term
|
Definition
| combination of carbamoyl phosphate and ornithine, by ornithine transcarbamoylase |
|
|
Term
| What happens with Argininosuccinate synthetase? |
|
Definition
| citrulline combines with an asparate to create Argininosuccinate in a two step process |
|
|
Term
| Argininosuccinate is cleaved into? |
|
Definition
cleaved by
argininosuccinase to arginine and
fumarate. |
|
|
Term
|
Definition
arginine to urea
and ornithine, found only in liver. |
|
|
Term
| What is the aspartate-argininosuccinate shunt? |
|
Definition
| the connection between CAC and Urea cycle. |
|
|
Term
| What does N-acetylglutamate do? |
|
Definition
allosteric
activator of carbamoyl phosphate
synthetase. |
|
|
Term
| What is the cost of Urea synthesis? |
|
Definition
| 4 phosphates but after NADH reproduction only 1.5 ATP |
|
|
Term
| What two things are used to treat deficiencies in urea cycle enzymes? |
|
Definition
Benzoate and phenylbutyrate
b/c they use up glycine and glutamine |
|
|
Term
| What two amino acids are only ketogenic? |
|
Definition
|
|
Term
| What is unique about tetrahydrofolate? |
|
Definition
| can transfer differing reduction forms of Carbon |
|
|
Term
| What three groups play a big role in amino acid catabolism? |
|
Definition
| Biotin, Tetrahydrofolate and S-adenosylmethionine |
|
|
Term
| Lack of phenylalanine hydroxylase leads to? |
|
Definition
causes
defective neural development and
mental retardation. and PKU |
|
|
Term
|
Definition
| diet of PHe and Tyr. or supplement precursors |
|
|
Term
| What are the three pathways of glycine degradation? |
|
Definition
convert to serine, Cleaved to CO2, NH4+ and a methylene or converted in kidney to oxalic acid by D-amino acid oxidase
group or |
|
|
Term
| Maple Syrup Urine Disease is? |
|
Definition
defect in Branched
Chain α-keto Acid Dehydrogenase Complex. leads to alot of branched AA |
|
|
Term
| What enzyme performs oxidative phosphorylation on pyruvate? |
|
Definition
| Pyruvate dehydrogenase complex |
|
|
Term
| What do the 5 reactions of PDH do? |
|
Definition
| 1.) decarboxylates 2.)oxidize to carboxylic acid 3.) acetyl group is transferred from lipoyl group to CoA 4.)reduced lipoate is oxidized to original form 5.)Hydrogens is transferred to NAD |
|
|
Term
| What is the effects of Beriberi? |
|
Definition
| loss of neural function do to poor PDH function |
|
|
Term
| What is the overall result of CAC? |
|
Definition
| 3 NADH, 1 FADH2, 1 ATP(GTP) and 2 CO2 |
|
|
Term
| What are the intermediates of CAC? (9) |
|
Definition
1.)Acetyl-CoA and Oxaloacetate
2.) Citrate
3.) Isocitrate
4.) alpha-ketoglutarate
5.) Succinyl-CoA
6.)Succinate
7.) Fumarate
8.) Malate
9.) Oxaloacetate |
|
|
Term
| What is the process of citrate synthase? |
|
Definition
| OAA binds then opens the binding site for acetyl-CoA forms a thioester intermediate which is hydrolyzed |
|
|
Term
| How can aconitase proceed forward? |
|
Definition
| product (isocitrate) is used up immediately |
|
|
Term
|
Definition
| dietary iron carrier in blood, stored by ferritin |
|
|
Term
| What is the moonlighting effect of aconitase? |
|
Definition
it triggers Iron Regulatory Protein 1,
which binds to Iron Response Elements up taking more Fe |
|
|
Term
| What does isocitrate dehydrogenase do? |
|
Definition
| produces NADH, CO2 and alpha-ketoglutarate |
|
|
Term
| What does α-Ketoglutarate Dehydrogenase Complex produce? |
|
Definition
|
|
Term
| what does Succinyl-CoA Synthase do? |
|
Definition
| produce GTP/ATP and Succinate |
|
|
Term
| What does Succinate Dehydrogenase do? |
|
Definition
| Produces FADH2 and Fumarate |
|
|
Term
| what can compete with Succinate Dehydrogenase? |
|
Definition
|
|
Term
What does Fumarate Hydratase or
Fumarase do? |
|
Definition
|
|
Term
| Whats the products of Malate Dehydrogenase? |
|
Definition
|
|
Term
| How many cycles does the methyl Cardon of acetyl survive in CAC? |
|
Definition
|
|
Term
| When is the Carboxyl C of acetyl lost to CO2? |
|
Definition
|
|
Term
| What activates the most important anaplerotic enzymes? and how is it regulated? |
|
Definition
| Pyruvate carboxylase activated by acetyl CoA |
|
|
Term
| what activates PEP carboxylase? |
|
Definition
F1,6-BP,
which accumulates when CAC is slower than glycolysis. |
|
|
Term
| What are the two steps of biotin catalyzed reactions in pyruvate carboxylase? |
|
Definition
1.) bicarbonate is converted to the more activated CO2
2.) CO2 reacts with pyruvate to form oxaloacetate |
|
|
Term
|
Definition
PDH complex,
Citrate synthase,
Isocitrate DH, and
α-ketoglutarate DH |
|
|
Term
| what is the main regulator of PDH? |
|
Definition
| The Kinase is allosterically activated by ATP and it inacivates the E1 of PDH by phosphorylation |
|
|
Term
| What is the regulator of the first three steps of CAC? |
|
Definition
| products and ATP and Calcium for isocitrate DH/alpha-ketoglutarate DH |
|
|
Term
| What does excess citrate inhibit? |
|
Definition
| Phosphofruktokinase to slow down glycolysis that feeds CAC |
|
|
Term
| What enzyme is membrane bound in CAC? |
|
Definition
|
|
Term
| what is the Glyoxylate cycle? |
|
Definition
| a circular pathway that takes in two molecules of acetate and put out one molecule of succinate (glyoxysome) starts with glyoxylate not OAA |
|
|
Term
| What three enzymes are present in both CAC and Glyoxylate Cycle? |
|
Definition
Citrate synthase, aconitase, and
malate DH |
|
|
Term
| What are two unique enzymes to glyoxylate cycle ? |
|
Definition
Isocitrate lyase and malate
synthase, essential for this cycle,
are absent in vertebrates |
|
|
Term
| What is the branching point of CAC/glyoxylate cycle? |
|
Definition
| isocitrate lyase regulated by kinase/phosphatase |
|
|
Term
| What does the kinase ability do to isocitrate DH? |
|
Definition
shunts isocitrate to the
synthetic route to Glc via glyoxylate cycle |
|
|
Term
| Why does intermediates of CAC activate phosphatase ability? |
|
Definition
| to activate isocitrate DH (more CAC) |
|
|
Term
| What do AMP/ADP do to CAC? |
|
Definition
| inhibit the kinase which inhibits isocitrate DH |
|
|
