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Biochemistry > Week 1 - Introduction to Medical Biochemistry > Flashcards

Week 1 - Introduction to Medical Biochemistry Flashcards

1
Q

Xenobiotics

A

are foreign compounds the body must degrade or excrete before they accumulate or cause damage

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2
Q

Metabolites

A

typically small molecules that are intermediates in biochemical pathways or act as regulators of function.

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3
Q

glucose

A
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4
Q

Fructose

A
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5
Q

galactose

A
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6
Q

d-mannose

A
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7
Q

d-galactose (fisher projection)

A
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8
Q

sucrose

A

Glucose and fructose linked in an alpha(1-2) linkage. Table sugar, made from sugar cane or beets. sucrose is not a reducing sugar.

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9
Q

Lactose

A

Galactose and Glucose in a Beta (1-4) linkage. Milk sugar, digested by lactase in the gut in infants.

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10
Q

maltose

A

Two Glucose molecules in an alpha(1-4) linkage, the same linkage found in glycogen.

Results from starch/glycogen breakdown in the gut

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11
Q

maltodextrin

A

3 or more linearly joined glucose units in alpha(1-4) linkage

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12
Q

glycogen

A

Glucose storage in animals. Linear α(1→4) glucose chains, plus branches from by α(1→6) glycosidic bonds.

Glycogen differs from amylopectin in having more frequent branchings. This means more free ends, and a more hydrated dendrimer.

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13
Q

amylose

A

a linear, non-branched chain of glucose molecules connected by α(1→4) glycosidic bonds. Much less digestible (resistant starch) than amylopectin.

Amylose forms more compact, less hydrated structures, and is digested much slower (fewer end points, and the more compact, less hydrated structure makes it less accessible to digestive enzymes.

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14
Q

amylopectin

A

Glucose storage in plants that animals can digest. α(1→4) glycosidic bonds

with branch points of (1→6) glycosidic bond

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15
Q

cellulose

A

this is a dietary fiber. It is not digested to a significant extent in humans because we lack an enzyme to break the β(1-4) glycosidic bond, as do other mammals. Ruminants and beavers rely on gut micro-organisms to break down the cellulose into glucose as an energy source.

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16
Q

Blood antigens (composition)

A

Carb trees attached to lipids or proteins. The precise linkages and order, depends on individual proteins present and can vary among individuals. Therefore, recognition of carbohydrates as antigens can be an important aspect of immune recognition as foreign or self.

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17
Q

Chondroitin-sulfate

A

The Chondroitin-sulfate repeat provides a lot of negative charge to the sugar chains that

keeps them hydrated, and apart. This provides the elasticity required in connective tissue.

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18
Q

Charged Amino Acids - Anionic

A

Glu,Asp

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19
Q

Charged Amino Acids - Cationic

A

Arg,Lys,His

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20
Q

Polar Amino Acids

A

Ser,Thr,Gln,Asn,Cys

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21
Q

Non-polar Amino Acids

A

Leu,Ile,Met,Val,
Phe,Tyr,Trp(Aromatic)

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22
Q

Small Amino Acids

A

Ala,Glycine

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23
Q

Cyclic Amino Acids

A

Pro

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24
Q

primary structure protein

A

Proteins are typically described as N-terminus (free amino terminus) to C-terminal. Amino acids are conjoined through peptide bonds. Peptide bonds are amide bonds (bonds between a carboxylate group and an amine). The sequence of amino acids conjoined through peptide bonds.

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25
Q

Secondary structure proteins

A

Alpha-helices
Beta-sheets
Turns

Alpha-helices and beta-sheets, tend to maximize the hydrogen bonding in the core of the protein.

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26
Q

Tertiary protein structure

A

Organization of secondary structures into a domain – only a single peptide. Domain structures are held in place through hydrophobic interactions, disulfide bonds, ionic bonds (rare), and sometimes hydrogen bonds. There are a number of canonical domain structures that recur in many proteins.

For example, in myoglobin, the alpha-helices (secondary structure elements) assemble into a compact globin fold structures.

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27
Q

Quaternary structure

A

The assembly of domains or subunits into a functional protein unit. For example, hemoglobin is assembled from two alpha subunits and two beta subunits. Alpha and Beta subunits have very similar tertiary structures, the same globin fold as myoglobin. Hemoglobin, is therefore, an assembly of four subunits, each with a globin domain fold.

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28
Q

Purine

A

Adenine and Guanine are the purines (two rings)

29
Q

Pyrimidines

A

cytosine, thymine, and uracil are pyrimidines (one ring)

30
Q

Nucleotides (coposition)

A

Constituent:

  • Ribose (5-carbon sugar)
  • Made in Hexose Monophosphate shunt – Deoxy-ribose

Base:

  • Purines: Adenine, Guanine
  • Pyrimidines: Cytosine,Thymine,Uracil

Phosphate (backbone) in 5’ and 3’

31
Q

Amphipathic lipids

A

Many Lipids are amphipathic where the polar and non-polar parts are segregated within the

molecule. Amphipathic lipids are required constituents of micelles, vesicles, and bilayer sheets.

32
Q

Lipids

A
  • hydrophobic or amphiphilic small molecules occurring in nature.
  • Not soluble in water except as aggregates in the form of micelles or vesicles or membrane sheets. Even so, they are more properly referred to as dispersions rather than having been dissolved.
  • All lipids are non-polar to some extent.
33
Q

Waxes

A

long chain, branched hydro-carbons. Hydrophobic, solid, semisolid, or liquid. Completely non-polar biological molecules (waxes, triglycerides, cholesterol esters) tend to form solids or fat (unless they are small, like the hydrocarbons in gasoline).

34
Q

Oils

A

Hydrophobic liquid. Can be hydrocarbons, triglycerides, or fatty acids of varying length, but can be other chemical types as well.

35
Q

Fat

A

e.g triglycerides, hydrophobic, solid.

36
Q

Detergents

A

natural or synthetic amphiphilic compounds that act

as surfactants (form micelles).

37
Q

Catabolism

A

the conversion of complex food and storage molecules (complex carbohydrate, protein and fat) into simpler components (monosaccharides, fatty acids, aminoacids) that can be utilized for energy.

38
Q

Anabolism

A

The use of simple metabolites (simple sugars, fatty acids and amino acids) to generate more complex molecules for storage (glycogen, triglycerides, and protein) and for maintenance and growth (new proteins, membranes), including specialized molecules such as hemes, cholesterol, and nucleotides.

39
Q

Liver

A
  • stores glycogen, fat and protein
  • maintains blood levels of glucose
  • makes glucose and synthesize fat
  • detoxifies
40
Q

muscle

A
  • major stoage for glycogen and protein
  • muscle lacks glucose-6-phosphatase and cannot make glucose for other organs
  • d/t glycogen storage muscle can function anaerobically
41
Q

adipose tissue

A
  • tissue serves as the major storage site for triglyceride (FAT)
42
Q

Kidney

A
  • specializes for nitrogen metabolism and excretion of urea
43
Q

intestine

A
  • serves to absorbe nutrients from digested food and pass them on to blood and liver
44
Q

red blood cells (erythrocytes)

A
  • function only anaerobically
  • specialized in oxygen delivery
45
Q

brain

A
  • uses glucose as fuel and metabolizes little fat
  • can use ketone for fuel during long fast or starvation
46
Q

Glycolysis

A

The transformation of glucose (in cyctoplasm) to pyruvate; generates small amount of energy quickly.

Exergonic steps are regulatory steps & irreversible:

  • Hexokinase
  • Phosphofructokinase
  • Pyruvate Kinase
47
Q

Fates of Pyruvate

A
  • Lactate (anaerobic metabolism)
  • AcetylCoA – aerobic energy production, fatty acid synthesis
  • Oxaloacetate – anapleurotic reactions (refilling of TCA intermediates) or the first reaction point of gluconeogenesis (Liver glucose production)
  • Ethanol – in microorganisms during fermentation.
  • Alanine – Nitrogen transport
48
Q
A
49
Q

TCA cycle

A

Breakdown of Acetyl (Acetyl CoA) to CO2 with production of reducing equivalents (NADH and CoQH2. Occurs in the mitochondria.

50
Q

Oxidative Phosphorylation

A

electron transport. Converts high energy electrons (reducing power) to ATP and makes water from oxygen.

51
Q

Pyruvate Dehydrogenase

A

PDH A major regulated step

  • Has a number of important vitamins and cofactors. Deficiency in these causes metabolic problems.
  • Regulates movement of pyruvate to Acetyl CoA.
  • Regulates by Acetyl CoA, NADH, and by phosphorylation.
  • Regulated indirectly by hormones
52
Q

Sources Acetyl CoA

A
  • Pyruvate
  • Beta-oxidation of fatty acids
  • Ketone bodies
53
Q
A
54
Q

Fates of AcCoA

A
  • TCA cycle entry
  • FA synthesis
  • Ketone body production
55
Q

Acetyl CoA in TCA cycle

A
  • Serve as start points in anabolic reactions
  • Serve as end points for catabolism of many amino acids
  • Are involved in other pathways and transport mechanisms
56
Q

Major Metabolic Pathways for Fatty Acid Degradation

A
  • β-Oxidation: The breakdown of fatty acids to Acetyl CoA; this takes place in the mitochondria. It ultimately makes energy (ATP) from fat stores.
  • TCA cycle – Breakdown of Acetyl (Acetyl CoA) to CO2 with production of reducing equivalents (NADH and CoQH2. In mitochondria
  • Oxidative Phosphorylation – electron transport. Converts high energy electrons (reducing power) to ATP and makes water from oxygen.
57
Q

TCA cycle output

A
  • GTP
  • 3 NADH
  • 1 FADH2 (CoQH2)
  • 2 CO2
  • TCA cycle produces reducing equivalents in the form of NADH, and CoQH2.
  • • TCA cycle produces 1 ATP equivalent as GTP.
  • • TCA cycle produces 2 CO2 from Acetyl CoA.
58
Q

TCA cycle regulation

A

Enzymatic at the following enzymes

  • Citrate synthase
  • Isocitrate dehydrogenase
  • Alpha-ketoglutarate dehydrogenase

By limiting cofactors (NADH in particular)

By ATP and ADP concentrations in the mitochondrion.

By Mass action coupling to oxidative phosphorylation.

59
Q

Gluconeogenic Precursors

A
  • Lactate – from anaerobic glycolytic metabolism
  • Alanine and glutamine from Protein breakdown.
  • Glycerol from fat breakdown.
  • Other products that feed into the TCA cycle.
60
Q

3 general mechanism for Metabolism Regulation

A
  • metabolite
  • Phosphorylation
  • Changes in protein activity
61
Q

Metabolite - metabolism regulation

A
  • Feedforward, feedback inhibition or activation
  • Cofactor/substratere striction
  • Allosteric protein regulation
62
Q

Phosphorylation feedback regulation

A

OftenHormoneMediated
• Insulin (generally dephosphorylates)
• Glucagon – Activates protein Kinase A

63
Q

Changes in protein activity metabolism regulation

A
  • Changesintranscription/translation
  • Changesindelivery(glucosetransporter)
64
Q

Insulin

A

promotes Glucose uptake

– Glut4 Glucose transporters are moved from internal vesicular stores to the plasma membrabe. Glut4, is delivered from internal vesicle stores to the plasma membrane to increase glucose uptake in response to insulin stimulation.

65
Q

Starch

A

consists of a mixture of Amylose and amylopectin.

  • Amylopectin (branched) Glucose storage in plants that animals can digest. α(1→4) glycosidic bonds with branch points of (1→6) glycosidic bonds.
  • Amylose – a linear, non-branched chain of glucose molecules connected by α(1→4) glycosidic bonds. Much less digestible (resistant starch) than amylopectin. Amylose (linear) forms more compact, less hydrated structures, and is digested much slower (fewer end points, and the more compact, less hydrated structure makes it less accessible to digestive enzymes.
66
Q

Phosphatidyl ethanolamine

A

One of the primary roles for phosphatidylethanolamine in bacterial membranes is to spread out the negative charge caused by anionic membrane phospholipids. … It acts as a ‘chaperone’ to help the membrane proteins correctly fold their tertiary structures so that they can function properly.

67
Q

Phosphatidyl Inositol

A

Phosphorylated forms of phosphatidylinositol (PI) are called phosphoinositides and play important roles in lipid signaling, cell signaling (calcium signaling) and membrane trafficking. The inositol ring can be phosphorylated by a variety of kinases on the three, four and five hydroxyl groups in seven different combinations.

68
Q

Phosphatidyl Serine

A

Alzheimer’s disease is a form of dementia that can rob people of the ability to think clearly, perform everyday tasks and, ultimately, remember who they even are. Phosphatidylserine supplements may increase levels of brain chemicals involved with memory and improve brain cell communication.

69
Q
A

Biochemistry (3 decks)

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