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PHD > BCH 100 Final Prep > Flashcards

BCH 100 Final Prep Flashcards

1
Q

What are Nucleotides for?

A

-Signaling
-Carrying Chemical Energy
-Cofactor Components
-Building blocks for Nucleic Acids

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2
Q

Why do we need Amino Acids?

A

Precursor for proteins, Biomolecules and energy

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3
Q

How is an Amino acid catabolized?, What is the enzyme?

A

The amine group is removed by an -ketoglutarate to become glutamate and an -keto acid, Aminotransferase

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4
Q

Why are Glutamine and Alanine necessary in the blood?

A

They carry toxic amine groups through the blood to the liver to be excreted

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5
Q

Draw Urea

A

H2N-(C=O)-NH2

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6
Q

Why does the Urea cycle happen and where does it occur?

A

The detoxification and exretion of excess NH4+, in the liver

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7
Q

Write the Urea Cycle

A

Week 10 Lec 24

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8
Q

Name the Essential Amino acids

A

Valine
Leucine
Isoleucine
Histidine
Lysine
Methionine
Threonine
Tryptophan
Phenylalanine

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9
Q

What are the two major ways Nitrogen is incorporated into the food chain?

A

Nitrogen-fixing bacteria converting atmospheric Ns to NH4+, Nitrogen-assimilating Plants and Bacteria conveting NO3- to NO2- to NH4+

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10
Q

What is Negative nitrogen balance?

A

If you are missing even one essential amino acid your body will keep eating through the protiens you have trying to find it, and you end up with such a large increase in Urea that you have more nitrogen leaving than coming in

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11
Q

What is a Hormone?

A

an intercellular Chemical Messenger produced in the ductless glands of the endocrine system

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12
Q

Name four hormones types and give examples

A

Steroids: estrogen, androgens
Polypeptides: insulin, glucagon
Amino acid derivitiives: Epinephrine (adrenaline)
Fatty acid derivatives: Prostaglandis

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13
Q

What are the three different hormone systems?

A

Endocrine (travel through blood)
Paracrine (travel to nearby cells)
Autocrine( targets the same cell)

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14
Q

How do Hormones function?

A

They bind to a specific receptor on or in the target cell membrane, triggering a signal cascade that can alter enzyme activity or alter gene transcription

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15
Q

What are the three major classes of membrane receptors?

A

7-Transmembrane a.k.a. G-protien coupled receptors
Dimeric membrane recepters that recruit protien kinases
Dimeric protien receptors that ARE protien kinases

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16
Q

Explain a GPCR cascade of Epinephrine

A

-Ep binds to the beta-adrenergic receptor -
-on the other side of the receptor in the membrane a G protien exchanges a GDP for a GTP and an alpha G dissociates from a betagamma G.
-Alpha G-GTP activates adenylate cyclase which converts ATP to cyclic AMP (cAMP), which is the second messenger that activates protein kinase A

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17
Q

How is GPCR regulated?

A

-Reciprocal regulation
-Active glycogen breakdown
-inactive glycogen synthesis

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18
Q

How is the signal cascade stopped?

A
  1. No more signal
  2. Break down of cAMP, hydrolyzed by cyclic nucleotide phosphodiesterase back into AMP
  3. a built in timing mechanism of GTP on alpha G slowly hydrolyzing to GDP
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19
Q

How is RTK activated?

A

Binding to an RTK receptor causes it to autophosphorylate its own tyrosine residues, phosphotyrosines allow binding and phosphorylation of the receptor substrate causing a cascade

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20
Q

How is RTK regulated?

A

-stopping the hormone signal
-Removal of phosphates from activated proteins,

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21
Q

Describe Glucagon

A

-29-amino acid polypeptide hormone
-Released by alpha-cells of islets of langerhans in the pancreas
-Signal for low blood sugar (starvation state)
-Binds to GPCRs on liver cells

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22
Q

Describe Epinephrine

A

-Derived from Tyrosine in adrenal medulla
-Fight or flight hormone
-Acts on GPCRs of the liver and muscle cells

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23
Q

Describe Insulin

A

-Peptide hormone
-Released by beta-cells of islets of langerhans (pancreas)
-Signal for high blood glucose (“fed” state)
made as preproinsulin, undergoes proteolytic cleavage
-chains held together by disulfide bonds
-Binds to RTK (NOT GPCR)

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24
Q

Describe a lipoprotien and its functions

A

Lipoprotiens transport TAGs and Cholesteral in the blood. The protein part solubilized lipids and direct the particle, the lipid parts are the fats that need to be transported

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25
Q

What are the categories of Lipoprotiens?

A

Chylomicrons: dietary fat (TAG) transport
VLDL: very low density endogenous fat (TAG) transport
LDL: low density, major cholesterol carrier in blood
HDL: high density: reverse cholesterol transport

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26
Q

Why does the oxidation of fats yield more energy that oxidation of carbs?

A

Fatty acids are highly reduced

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27
Q

What are the ways and locations triacylglycerol used?

A

When broken down into glycerol:
-it can enter the liver to go through glycolysis and become pyruvate or gluconeogenesis to become glucose.
When broken into a fatty acid:
it enters other tissues to go through beta oxidation and the citric acid cycle

28
Q

Draw the beta oxidation cycle

A

Week 9 lec 21-22

29
Q

How many NADH, FADH and GTP is made per cycle of Beta oxidation?

A

1NADH, 1 FADH

30
Q

How many ATP per NADH and FADH?

A

2.5 NADH, 1.5 FADH

31
Q

Where are ketone bodies made and under what circumstances?

A

Liver Mitochondria, ketosis happens High fat intake, low sugar, starvation and diabetes

32
Q

Name 3 ketone bodies

A

-Acetoacetate
-Acetone
-Beta hydroxybutyrate

33
Q

Name the 12, 14, 16, and 18 carbon fatty acids

A

12-Laurate
14-Myristate
16-Palmitate
18-Stearate

34
Q

What is a lipid?

A

An organic molecule that is not soluble in water, but is soluble in organic solvents

35
Q

What are the 5 main classes of fatty acid and their purposes?

A
  1. Free fatty acids: Fuel
  2. Triacylglycerols: Storage or fatty acids
  3. Phospholipids: Membrane lipids
  4. Glycolipids: membrane partly made of carbohydrates
  5. Steroids: polycylic hydrocarbons with a variety of functions
36
Q

How and where is fatty acid activated?

A

Fatty acid is activated by acyl-CoA synthase and occurs in the cytoplasm

37
Q

How does activated fatty acid get into the mitochondria and what are the steps?

A

The carnitine shuttle transports fatty acid into the mitochondria:
1. carnitine acyltransferase -1 (CAT-1) transfers acyl to the carnitine
2. Carnitine translocase carries acylcarnitine into the matrix
3. CAT-2: transfers acyl from carnitine to CoASH to regenerate Acyl-CoA

38
Q

Draw The Calvin Cycle

A

Week 8 lec 19

39
Q

Define Photosynthesis

A

Using light energy to biosynthesize sugar

40
Q

Draw the light dependent photosystem

A

Week 8 lec 19 (lower part)

41
Q

Draw the electron transport chain

A

Week 7 lec 18

42
Q

Whats the difference between a Nucleosides and Nucleotides?

A

Nucleosides: Base + sugar
Nucleotides: Base + sugar + Phosphate

43
Q

Whats the difference between Purines and Pyrimidines?

A

Purines: Two heterocyclic rings
Pyrimidines: one Heterocyclic ring

44
Q

Name the Purines

A

Purine, adenine, and Guanine

45
Q

Name the Pyrimidines

A

Pyrimidine, Cytosine, Uracil, Thymine

46
Q

What are the differences between purine and pyrimidine biosynthesis?

A

Purine synthesis: Start with sugar, build ring on ie
Pyrimidine synthesis: Build base ring, add sugar

47
Q

What are the two way to make nucleotides?

A

-Salvage pathways where you recycle nucleoside
-De Novo synthesis where you make them from scratch

48
Q

What is the committed step of Pyrimidine synthesis

A

Aspartate Transcarbamoylase

49
Q

What is the committed step of Purine Synthesis

A

PRPP-gln amidotransferase

50
Q

Draw Orotate

A

6 atom ring: 1N,2C,3N,4-6C

51
Q

Draw Glycine

A

Amino acid slide

52
Q

What do enzymes change and not change?

A

They change delta-G double dagger, the transition energy also known as the activation energy.
They do NOT change delta-G (also written delta-g rxn), the reaction energy

53
Q

On a reaction rate graph, what do the following mean?
V0
Vmax
K m
K cat

A

V0: initial velocity
Vmax: Maximum Velocity
K m: Substrate concentration at 1/2 Vmax
K cat: turnover number

54
Q

On a Lineweaver-Burk graph what are:
X axis:
Y axis:
X-intercept:
Y-intercept:
Slope:

A

X axis: 1/[S]
Y axis: 1/V0
X-intercept: -1/Km
Y-intercept:1/Vmax
Slope: Km/Vmax

55
Q

How do the three types of inhibitors affect the Lineweaver-Burk graphs?

A

Competitive shift slope but keeps y-intercept
Uncompetitive shifts the intercepts but not the slope
Noncompetititve shifts the slope but not the x-intercept

56
Q

What naming monosaccharides, what does D and L mean?

A

From the last carbon, is the nearest alcohol up the chain to the right (D), or the left (L)

57
Q

whats the name of a 5-ring sugar and a 6 ring sugar?

A

5: Furanose
6:Pyranose

58
Q

How are Oligosaccharides connected?

A

O-glycosidic bonds

59
Q

Define Maltose structure

A

Two cyclic glucose connected by a alpha(1,4) bonds

60
Q

Define Lactose Structure

A

cyclic Galactos and cyclic glucose connected by beta(1,4) bond

61
Q

Define Sucrose structure

A

Cyclic glucose and cyclic fructose connected by alpha(1,2) bond

62
Q

Draw Fructose

A

Sugar structure handout

63
Q

Draw Galactose

A

Amino Structure handout

64
Q

What is the order for Purine nucleotide synthesis?

A

-PRPP synthetase
-Glutamine-PRPP amidotransferase
-Inosinate Formation
-Ribonucleotide Reductase

65
Q

Draw Succinate

A

COO- _CH2_CH2_COO-

66
Q

Draw Pyruvate

A

COO-_C=O_CH3

PHD (7 decks)

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