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Biochemistry II test #3 study guide

by: ChasePrater

Biochemistry II test #3 study guide 4510

Marketplace > Middle Tennessee State University > 4510 > Biochemistry II test 3 study guide
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This study guide is detailed questions (with answers) that I have made as I studied the powerpoints along with information from lecture and the book. It is over chapter 20 and most of 21. I apologi...
Biochemistry II
Dr. Ooi
Study Guide
biochemistry, Biochemistry II, amino acid metabolism, Fat metabolism, fatty acid biosynthesis
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This 5 page Study Guide was uploaded by ChasePrater on Sunday March 27, 2016. The Study Guide belongs to 4510 at Middle Tennessee State University taught by Dr. Ooi in Spring 2016. Since its upload, it has received 136 views.


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Date Created: 03/27/16
Biochem  2  Studyguide  #3     1.  Why  are  triglycerides  a  better  energy  storage  molecule  than  glucose?   • Their  carbons  have  lower  oxidation  states,  and  they  are  nonpolar   molecules  so  they  are  stored  in  an  anhydrous  form  whereas  glucose  is   stored  in  a  hydrated  form.  This  means  that  you  get  more  energy  for  a   given  weight.     2.  What  is  Beta-­‐oxidation?   • The  process  of  breaking  down  a  fatty  acid  to  acetyl  CoA   3.  What  are  bile  salts,  and  what  is  their  main  function?   • amphipathic  cholesterol  derivatives  made  in  the  liver  that  act  like   detergents  to  break  apart  big  globs  of  fat  in  the  small  intestine  into   smaller  micelles.     • They  increase  the  lipid-­‐water  interface  so  that  digestion  can  be  rapid.   4.  What  are  the  two  types  of  lipases,  and  where  are  they  found?   • Pancreatic  lipase:  found  in  small  intestine   • Lipoprotein  lipase:  found  in  blood  of  muscle  and  adipose  capillaries.     5.  What  is  interfacial  activation?   • The  phenomenon  that  when  pancreatic  lipase  encounters  the  lipid-­‐water   interface,  its  activity  greatly  increases.     6.  What  is  the  role  of  intestinal  fatty  acid-­‐binding  protein?   • Protect  cells  from  the  detergent  like  properties  of  fatty  acids,  and  increase   fatty  acid  solubility.     7.  List  the  steps  of  lipid  transport  after  they  have  been  absorbed  by  intestinal   mucosa.   • Packaged  into  chylomicrons,  released  into  intestinal  lymph,  move  through   lymphatic  vessels  and  into  large  veins,  delivered  to  capillaries  of  skeletal   muscle  or  adipose  tissue.     8.  Cholesterol  delivered  to  liver  by  chylomicrons  is  incorporated  into  which   lipoprotein?   • VLDL   Where  are  fatty  acids  activated,  and  what  enzymes  do  this?   • For  mitochondrial  oxidation:  happens  on  outer  mito  membrane,  and  is  done   by  acyl-­‐CoA  synthetases  (thiokinases)   • For  peroxisomal:  also  done  by  acyl-­‐CoA  synthetases   What  determines  the  rate  for  fatty  acid  oxidation?   • Transport  of  fatty  acid  chains  across  the  inner  mitochondrial  membrane.     What  is  the  first  committed  step  of  fatty  acid  synthesis?   • Stage  2;  carboxylation  of  acetyl-­‐CoA   What  is  the  enzyme  in  this  step  and  how  is  it  regulated?   • Acetyl-­‐CoA  carboxylase.   • Allosterically  stimulated  by  citrate,  and  inhibited  by  long  chain  fatty  acyl-­‐ Coa’s     •   inactivated  when  phosphorylated  by  AMPK,  which  is  activated  by  ADP     and  inactivated  by  ATP.     •   Hormonal  control:  Insulin  removes  phosphate  (activiating  synthesis);     glucagon  and  epinephrine  promote  phosphorylation.   Which  two  enzymes  use  NADPH  in  fatty  acid  synthesis?   • Beta-­‐ketoacyl-­‐ACP  reductase  and  enoyl-­‐ACP  reductase   What  is  the  major  product  of  the  fatty  acid  synthesis  pathway,  and  what  are  the  total   reactants  needed?   • Palmitic  acid   • 8  acetyl-­‐Coa,  14  NADPH,  and  7  ATP   Where  does  beta-­‐oxidation  and  FA  synthesis  occur?   • beta-­‐oxidation:  mitochondria   • FA  synthesis:  cytosol   What  is  an  example  of  a  fatty  acid  that  we  cannot  produce?   • Linoleic  acid  (omega-­‐6)   What  enzyme  uses  coenzyme  B12,  and  what  is  special  about  this  coenzyme?   • Methylmalonyl  CoA  mutase   • It  contains  a  rare  carbon-­‐metal  bond   Does  the  carbon  in  the  CO2  produced  during  FA  synthesis  come  from  acetyl-­‐Coa  or   malonyl-­‐Coa?   • Malonyl-­‐Coa   What  is  the  acyl  carrier  in  beta-­‐oxidation  and  FA  biosynthesis?   • Beta-­‐oxidation:  CoA   • FA  biosynthesis:  ACP   At  what  carbons  of  a  FA  chain  can  we  not  introduce  double  bonds?   • C12  and  C15   At  the  beginning  of  triglyceride  synthesis,  what  organelles  use  G3P  and/or  DHAP  to   form  the  glycerol  backbone?   • Mito.  Uses  G3P   • Peroxisome  uses  DHAP   • ER  can  use  both.   What  is  formed  when  G3P  is  acylated  once?  And  then  a  second  time?   • 1  lysophosphatidate,  2  forms  phosphatidate  (a  diacylglyceride)   What  type  of  glycerophospholipids  contains  a  vinyl  ether  linkage  instead  of  an  ester   linkage?  Where  is  this  glycerophospholipid  synthesized?   • Plasmolagens;  made  in  peroxisomes   What  are  the  precursors  for  ceramide?   • Palmitoyl-­‐Coa  and  serine   What  are  the  head  groups  for  cerebrosides/gangliosodes?   • Cerebrosides:  1  sugar  (monosaccharide)   • Gangliosides:  many  sugars  (oligosaccharide)  +  sialic  acid   What  is  cholesterol  a  precursor  for,  and  what  is  its  structure?   • Steroid  hormones  (most  important)  and  bile  salts.   • 4  fused  rings;  3  six  member  rings  and  1  five  member  ring   Where  do  the  carbons  in  cholesterol  come  from?   • Acetate,  which  comes  from  acetyl-­‐CoA   What  is  the  first  committed  step  of  cholesterol  biosynthesis?   • Reduction  of  HMG-­‐CoA  to  mevalonate.     • This  step  requires  2  NADPH,  and  occurs  on  membrane  of  smooth  ER  in  liver   What  is  a  key  building  block  of  cholesterol  synthesis?   • Isopentenyl  pyrophosphate   What  other  molecules  are  made  from  this?   • Terpenes   • Vit  K   • Coenzyme  Q   • Chlorophyll   • Carotenoids   How  is  cholesterol  synthesis  regulated?   • By  regulating  HMG-­‐CoA  reductase   • Short  term:  phosphorylation,  which  is  controlled  by  cAMP  dependent  kinase.   Glucagon  inhibits  and  insulin  activates.  Active  when  dephosphorylated.   • Long  term  (primary  control):  the  concentration  of  cholesterol  controls  the   rate  of  enzyme  synthesis  and  degradation.  Enzyme  synthesis  is  inhibited  by   derivatives  of  mevalonate  and  dietary  cholesterol.     How  is  cholesterol  storage  regulated?   • ACAT  esterifies  cholesterol  so  it  can  be  stored.   • Activated  by  high  levels  of  cholesterol.               What  stimulates  the  release  of  hydrochloric  acid  and  pepsinogen?   • Gastrin   When  is  the  hormone  secretin  released,  and  what  does  it  do?   • When  acidic  contents  enter  the  small  intestine;  it  causes  pancreas  to  release   bicarbonate  to  bring  pH  back  to  7.     Why  do  we  degrade  internal  proteins?   • Use  carbon  skeletons  as  energy  during  starvation   • Get  rid  of  abnormal  proteins   • Allow  regulation  of  metabolism.   Why  is  it  important  that  lysosomal  enzymes  have  acidic  pH  optima?   • Since  these  dangerous/highly  active  enzymes  are  inactive  in  cytosolic  pH,  the   cell  is  not  harmed  if  the  lysosome  leaks.   What  sequence  do  most  proteins  have  that  are  degraded  in  lysosomes?   • Lys-­‐Phe-­‐Glu-­‐Arg-­‐Gln  (KFERQ)   What  types  of  proteins  are  degraded  through  ubiquitination  (cytosolic  degredation)   and  how  are  they  marked?   • Defective  proteins,  and  proteins  with  short  half  lives   • They  are  marked  for  degradation  by  covalently  linking  them  to  several   ubiquitins  via  an  isopeptide  bond.           What  types  of  proteins  are  degraded  by  lysozymes?   • membrane  proteins,  extracellular  proteins,  and  proteins  with  long  half-­‐lives.   What  determines  the  half  life  of  proteins?   • The  N-­‐terminal  residue.   • Short  half  lives:  asp,  arg,  leu,  lys,  and  phe   • Long  half  lives:  ala,  gly,  met,  ser,  and  val   What  is  a  PEST  sequence?   • A  12-­‐60  residue  section  of  a  protein  that  has  a  lot  of  Pro  (P),  Glu  (E),  Ser  (S),   and  Thr  (T).     • Proteins  with  this  are  degraded  rapidly.   What  amino  acids  (AAs)  are  susceptible  to  being  oxidized?   • Lysine,  arginine,  and  proline   What  is  the  first  step  in  AA  degradation?   • Deamination   What  are  the  two  mechanisms  for  deamination?   • Transamination,  and  oxidative  deamination   What  is  the  main  amino  group  acceptor  in  transamination?   • Alpha-­‐ketoglutarate   Where  does  oxidative  deamination  occur?   • Liver  mitochondria.   Does  Glutamate  dehydrogenase  use  NAD  or  NADP?   • Both   Where  does  the  urea  cycle  take  place?   • The  mitochondria  and  cytosol  of  the  liver   What  types  of  animals  get  rid  of  ammonia  by  converting  it  to  uric  acid?   • Birds  and  reptiles   Where  do  the  first  and  second  nitrogen  atoms  of  urea  come  from?   • 1  comes  from  NH4+  2  comes  from  aspartate  in  reaction  3.   What  do  the  BUN  levels  tell  you?   • If  BUN  levels  are  high  then  you  have  a  kidney  problem,  if  they  are  low  you   have  a  liver  problem.     How  is  urea  cycle  regulated?   • CPS  I:  allosterically  activated  by  N-­‐acetylglutamate,  which  is  made  from   glutamate  and  acetyl-­‐Coa.   • During  starvation  or  muscle  breakdown  a  lot  of  glutamate  is  made,  which   increases  amounts  of  N-­‐acetylglutamate   • Other  enzymes  are  controlled  by  substrate  availability.   • Long-­‐term  regulation  is  rate  of  enzyme  synthesis  and  breakdown   What  are  glucogenic  AAs  converted  to?   • Pyruvate,  alpha  ketoglutarate,  succinyl-­‐Coa,  fumarate,  or  OAA       What  are  ketogenic  AAs  broken  down  to?   • Acetyl-­‐Coa  or  acetoacetate   What  are  the  purely  ketogenic  AAs?   • Lysine  and  leucine   Which  AAs  make  up  the  pyruvate  family,  and  which  one  is  both  keto  and  glucogenic?   • alanine,  cysteine,  glycine,  threonine,  and  serine   • Threonine  is  both.     What  enzyme  acts  as  a  chemotheroputic  agent,  in  addition  to  aiding  in  AA   breakdown?   -­‐ L-­‐asparginase   Which  carbon  carrier  is  more  versatile,  and  what  does  it  derive  from?   -­‐ THF,  and  comes  from  folic  acid.   What  are  the  branched-­‐chain  AAs  and  where  are  they  broken  down?   -­‐ isoleucine,  leucine,  and  valine.   -­‐ They  are  broken  down  in  muscle,  adipose,  kidney,  and  brain  instead  of   liver.     Are  they  keto  or  glucogenic?   -­‐ isoleucine  and  valine  are  glucogenic   -­‐ leucine  is  both.   What  is  the  regulatory  step  of  brached-­‐chain  AA  breakdown?   -­‐ step  two:  oxidative  decarboxylation  via  BCKDH   What  are  the  products  of  lysine  degradation?   -­‐ acetoacetate  and  HMG-­‐Coa   The  breakdown  of  which  AA  involves  the  Kynurenine  pathway?   -­‐ tryptophan.   What  are  the  products  of  tyrosine  and  phenylalanine  breakdown?   -­‐ fumarate  and  acetoacetate   What  are  the  four  common  precursors  of  all  nonessential  AAs,  except  for  tyrosine?   -­‐ pyruvate,  OAA,  alpha-­‐ketoglutarate,  and  G3P   What  is  the  nitrogen  donor  for  synthesis  of  asparagine?   -­‐ glutamine   How  is  glutamine  synthesis  regulated?   -­‐ high  levels  of  alpha-­‐ketoglutarate  activate,  so  ammonia  levels  don’t  get   too  high.     -­‐              


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