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1st Year Veterinary Cards - Semester 1 > Biochemistry > Flashcards

Biochemistry Flashcards

1
Q

What are the functions of enzymes, are they anabolic or catabolic? How do they lower activation energy?

A

Biological catalysts, diagnostic tests
Both
Bring molecules closer together, reduce repulsion

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2
Q

What do active sites do? What are multi-enzyme complexes?

A

Bind with substrate, make/break chemical bonds

Aggregation of several co/enzymes

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3
Q

What are isoteric enzymes?

A

Enzymes which rate of reaction increases with substrate concentration (until saturation)

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4
Q

What are allosteric enzymes?

A

Enzymes which bind with an allosteric site, induces a change in the enzyme and allows easier binding (sigmoidal shape curve)

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5
Q

What is cooperativity?

A

The binding of an enzyme which changes the structure of the active site, which triggers the same in other active sites

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6
Q

What are the 3 types of inhibitors? Where do they bind to?

A

Competitive - active site
Non-competitive/allosteric - binds to allosteric site
Uncompetitive - binds to ES complex

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7
Q

What factors affect enzyme activity?

A

Temperature, concentration, pH, post-translational modification, coenzymes, cofactors

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8
Q

What are post-translation modifications?

A

Changes in the structure of an enzyme

Can be proteolytic activation (activates other enzymes) or phosphorylation

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9
Q

What are proteinase?

A

Enzymes which cleave proteins, can cause proteolytic activations

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10
Q

What are isoenzymes?

A

Different forms of an enzyme which catalyse the same reaction

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11
Q

What are the 4 stages of the nitrogen cycle? What happens in each stage?

A

Nitrogen fixation - nitrogen fixing bacteria convert N gas
Ammonification - conversion to ammonia by saprobionts
Nitrification - conversion to nitrates by nitrifying bacteria
Denitrification - conversion to gas in anaerobic conditions by bacteria

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12
Q

How many amino acids are there?

A

21

1 is rare

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13
Q

How do animals obtain essential and non-essential amino acids?

A

Essential - diet

Non-essential - biosynthesis

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14
Q

What are the functions of amino acids?

A

Build protein
Energy
Neurotransmitters

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15
Q

Amino acids can be ketogenic or glucogenic. What do these 2 terms mean? What happens after this?

A

Converted to ketones or glucose
Broken down to intermediates of acetyl CoA
Enter Krebs cycle

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16
Q

What are ureotelic animals?

A

Animals which produce urea

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17
Q

Where is urea excreted?

A

Kidneys, saliva, sweat

GI in ruminants - used to synthesise AAs as no protein in diet

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18
Q

What are urioctelic animals? Give examples?

A

Animals which excrete uric acid

Birds/reptiles

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19
Q

What are ammonotelic animals? Give examples

A 
Animals which can directly excrete ammonia
Aquatic animals (cartilaginous fish are both ammonetlic and ureotelic)
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20
Q

What are the stages of protein synthesis?

A

DNA transcribed to mRNA, then translated to a protein

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21
Q

What are the functions of proteins?

A

Structural - collagen, keratin, fibroin (silk/webs)
Movement - actin/myosin
Immune system - antibodies
Endocrine system - hormones/receptprs
Transport - haemoglobin, transferrin (glycoproteins in blood plasma)
Biocatalysts - enzymes

22
Q

Zwitterions are which type of isomer? What 2 forms can they be in?

A

Enantiomer

D or L - (L only in the body)

23
Q

What are the 4 protein structures?

A

1 - sequence of AAs held by peptide bonds
2 - H bonding between peptide bonds - alpha helix and beta pleated sheets
3 - H, disulfide, ionic bonds. 3D structures, metal ions between chains. Hydrophobic interactions
4 - interactions between subunits/polypeptide chains

24
Q

Proteins are mainly globular but can be fibrous or membranous. Give examples of each

A

Globular - enzymes/antibodies. Soluble, fold into compact molecules
Fibrous - multiple strands held by bonds, e.g. fibroin. 2 rows = protofilaments, dimerise to protofibrils, to microfibrils, then macrofibri;s
Membranous - channel/receptor proteins

25
Q

What is pregnancy toxaemia in sheep? What is a risk factor?

A

Blood poisoning from hypoglycaemia - high metabolic demand in last trimester of pregnancy
Excessive fat

26
Q

How do ruminants obtain glucose?

A

Gluconeogenesis

27
Q

Which carbohydrates are monosaccharides? Which are disaccharides?

A

Glucose, galactose, fructose

Maltose, lactose, sucrose

28
Q

Name 4 polysaccharides

A

Starch - amylopectin (branched) or amylose (coiled) chains of glucose in plants
Glycogen - like amylopectin, but in animals
Cellulose - straight chains of B glucose in plants
Chitin - chains of N-amide in fungi walls

29
Q

Which organ primarily controls blood glucose levels?

A

Liver

30
Q

Some glycogen storage disease are Van Gierkes, Pompe’s, Cori’s. What do these result in?

A

Hypoglycaemia

Hepatomegaly (liver enlargement due to glycogen)

31
Q

Which hormones do islets of Langerhans secrete?

A

Insulin - lower blood glucose. Promotes fat storage, B islets. Work by second messenger
Glucagon - increase blood glucose, a islets.

32
Q

What are the 3 types of diabetes?

A

Type 1- autoimmune, destroy islets. Symptoms emerge when most cells destroyed
Type 2 - obesity. Low insulin levels/ unresponsive.
Type 3 - Alzheimer’s disease due to insulin resistance in the brain

33
Q

What is hyperinsulinism? Why may this occur?

A

Abnormally high levels of insulin, results in hypoglycaemia.
Pancreatic tumours

34
Q

Why do many neonates get hypoglycaemia at birth? What induces enzymes which synthesise glucose?

A

Inadequate synthesis
Cold
Feeding

35
Q

What are the roles of lipids?

A 
phospholipid bilayer
Fuel
Insulation
Signalling molecules
Vit a/d/e/k
Nervous system
36
Q

What is arachidonic acid?

A

Fatty acid present in phospholipid bilayer

37
Q

What is cholesterol?

A

Precursor for lipid soluble hormones

38
Q

Describe the digestion and transport of lipids

A 
Bile salts emulsify fats
Degraded by intestinal lipases
Taken up by intestinal mucosa
FAs enter cells 
Chylomicrons enter blood stream
39
Q

What are chylomicrons?

A

Fat droplets that have been digested

40
Q

Where are lipids stored and released? What is the purpose of brown fat?

A

Adipose tissue

Thermogenesis

41
Q

Which multi enzyme complex is responsible for the biosynthesis of fatty acids?

A

Fatty acid synthase

42
Q

what is beta oxidation?

A

The breakdown of fatty acids to acetyl coA, which then enters the Krebs cycle.

43
Q

Where does beta oxidation take place? Is it anabolic or catabolic?

A

Mitochondria

Catabolic

44
Q

What is ketosis? What does it lead to? When might it be present?

A

Abnormally high levels of ketone bodies in the blood
Metabolic acidosis
Starvation, pregnancy toxaemia, acetonemia

45
Q

How many ATP are used and gained in glycolysis?

A

2 used

4 gained

46
Q

How are monosaccharides transported?

A

Na/Glucose transporters in intestinal epithelial cells

47
Q

In aerobic glycolysis, what is pyruvate converted to?

A

Acetyl coenzyme A

48
Q

In anaerobic glycolysis, what is pyruvate converted to? What happens to this after?

A

Lactate
Leaves muscles and travels to liver via blood
Converts lactate to glucose by gluconeogenesis

49
Q

What is gluconeogenesis?

A

The synthesis of glucose from non-carbohydrates e.g. lactate, glucogenic AAs
(Ruminants, starvation, intense exercise)

50
Q

What are the 2 types of muscles? What are their properties?

A
  1. Slow twitch, red, high myoglobin, little glycogen, oxidative
  2. Fast twitch, white, low myoglobin, high glycogen, glycolytic

1st Year Veterinary Cards - Semester 1 (54 decks)

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