Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

BIOL 311: Biochemistry I > Proteins (4), Carbohydrates (6/8), and Lipids (9) > Flashcards

Proteins (4), Carbohydrates (6/8), and Lipids (9) Flashcards

1
Q

Enzymes

A

Catalysts involved in biochemical reactions. Increase the rate of reaction without being consumed.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Substrates

A

Molecule that acts as the reactant in an enzymatic catalyzed reaction. Binds to the enzyme at the active site.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Active Site

A

The location where the enzyme binds to on the substrate which allows catalysis to occur.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Lock and Key model

A

Only the correct substrate will fit to he active site on the enzyme.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Induced Fit

A

Interaction of the substrate and enzyme helps form the active site.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Enzyme Classification: Oxidoreductases

A

Catalyze reactions involving the gain or loss of electrons.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Enzyme Classification: Transferases

A

Transfers one group to another

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Enzyme Classification: Hydrolases

A

Cleave a bond with water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Enzyme Classification: lysases

A

Break double bond with other means than oxidation and hydrolysis.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Enzyme Classification: Isomerases

A

Rearrangement of the molecule.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Enzyme Classification: Ligases

A

Join two molecules.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

The two assumptions of Michaelis-Menten Constant

A
  1. k2 is much slower than k-1, as this allows for the establishment of an equilibrium at the ES complex.
  2. The ES complex forms rapidly and exists at a relatively unchanging concentration as the reaction proceeds until substrates is depleted.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Vmax

A

Theoretical maximal velocity for a given concentration of enzyme.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

KM

A

Michaelis Constant: measures binding affinity of the ES complex.

  • Higher KM means lower affinity
  • Lower KM means higher affinity

KM = (k-1 + k2) / k1

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Michaelis-Menten Equation

A

vo = Vmax [S] / KM + [S]

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Lineweaver-Burke Plot

A

1/vo = (KM/Vmax)*1/[S] + 1/Vmax

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

kcat

A

Turnover Number: number of reactions the enzyme can catalyze per unit of time. Measures catalytic efficiency.

kcat = Vmax / [E]tot

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Diffusion Controlled Limit

A

Occurrence when rate-limiting step becomes the diffusion of enzyme and substrate together.

Rate must be between 10^8 and 10^9 M-1 sec-1.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Suicide Inhibitors

A

Covalently modifies the actives site of the enzyme, irreversibly block its function. Directly poisons the enzyme.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Competitive Inhibitors

A

Recognize molecules similar to the shape of the substrate that binds to the active site which competes directly with the substrates. Can be overcome with substrate concentration is high.

vo = Vmax * [S] / KM*a + [S]

a = 1 + [I] / KI

Dissociation Constant KI = [E][I] / [EI]

Increase KM and Vmax remains the same.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Uncompetitive Inhibitors

A

Binds to the ES complex

vo = Vmax * [S] / KM + [S]*a’

a’ = 1 + [I] / KI’

KI’ = [ES][I] / [ESI]

Decrease KM and Decrease Vmax.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Mixed Inhibitors

A

A combination of competitive and uncompetitive inhibitors.

vo = Vmax * [S] / KMa +[S]*a’

Decrease or Increase KM and Decrease Vmax.

Note: If a = a’, the line will intersect on the x-intercept with different Vmax but same KM. This is known as the non-competitive or pure mixed inhibition.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

General Principles of Enzyme Catalyzed Reactions

A
  • Enzymes bind to substrates with various weak forces (Van Der Waal, Ionic Bonding, Hydrogen Bonding, Dipole-Dipole Interaction) and entropy (delta S) decreases.
  • Enzyme binds to substrates with large number of weak forces known as electrostatic catalysis (sum total of the weak forces acting on the substrate).
  • In induced fit, enzyme bind substrates that favours the transition state.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Types of Catalysis: General acid-base catalysis

A

Amino acid side chains donate or accept protons. Polar and charged amino acids are important.

For example: Lysozyme (Glu and Asp)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

Types of Catalysis: Metal ion catalysis

A

Active site metal ion can act as a redox active center. Site can also act as a Lewis base or acid.

For example: Anhydrase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

Types of Catalysis: Covalent catalysis

A

Nucleophilic or electrophilic attack on an atom which results in a covalent intermediate. Involves Ser, Asp, Lys, Tyr, Cys, and other cofactors.

For example: Chymotrypsin (catalytic triad: Asp, Ser, His) and Chmotrypsinogen, the inactive form.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

Proteases

A

Enzyme that degrades proteins.
Many have Trypsin fold which are structures comprised of two Beta barrel domains, the active site being at the interface.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

Affinity Labeling

A

Technique used to specifically label residues on the active site. Label only one amino acid residue, suggesting that the label amino acid is not the same as other amino acid residues.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

Enzyme Regulation: Covalent modification -) Proteolytic cleavage

A

An inactive enzyme becomes active through cleavage or digestion of proteins and peptides (Irreversible)

For example: Chymotrypsinogen (an inactive form) is activated by proteolytic cleavage to Chymotrysin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

Enzyme Regulation: Covalent modification -) Phosphorylation

A

A form of protein activation, facilitated by protein kinases which add phosphate groups to the hydroxyl groups of serine, threonine, or tyrosine. Phosphatase remove phosphate groups. The regulation occurs through a series of singling steps termed a signalling cascade. (Reversible)

For example: Src

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

Enzyme Regulation: Allosteric Regulation

A

Increases and decreases the enzymatic activity by binding at a site other than the active site. Most rapid and most direct form of regulation. Relaxed and Tense.

32
Q

Monosaccharides Classifications

A
  1. Number of carbon
  2. Aldehyde vs Ketone
  3. Based on stereochemistry on penultimate carbon. D-isomer if hydroxyl on the right and L-isomer if hydroxyl on the left.
33
Q

Furanoses

A

5 Chair Conformation

34
Q

Pyranoses

A

6 Chair Conformation

35
Q

Epimer

A

Conformation when carbohydrates differ at one sterocenter

36
Q

Anomeric Carbon

A

Former carbonyl carbon (C-1 or C-2)

a - OH on bottom face of the ring
B- OH on top face of the ring

37
Q

Penultimate Carbon

A

Chiral carbon furthest away from the carbonyl besides the achiral carbon (C-5)

38
Q

Mutarotation

A

Converting from numeric form to the other (a to B or B to a)

39
Q

Haworth Projections

A

Monosaccharide in their cyclic form

40
Q

Chemically modified: Amino sugars

A

Hydroxyls group can be replaced by amine

41
Q

Chemically modified: Acylation

A

Addition of acyl group [R - C =O] ie: amine to amide

42
Q

Chemically modified: Sugar alcohols

A

Carbonyl group is reduced to alcohols which makes it impossible for sugar alcohol to form a cyclic structure.

43
Q

Chemically modified: Sugar acid

A

Monosaccharide can be oxidized, producing carboxylic acid modification.

44
Q

Chemically modified: Deoxy sugars

A

Removal of hydroxyl on one or more carbons of a monosaccharide.

45
Q

Monosaccharide

A

Glucose
Galactose
Fructose

46
Q

Disaccharide

A

Reducing Disaccharide contains aldehyde and ketone

Galactose + Glucose = Lactose (B-1,4 linkage)
Glucose + Fructose = Sucrose (a,B-1,2 linkage)
Glucose + Glucose = Maltose (a-1,4 linkage)

47
Q

Raffinose

A
  • Energy storage
  • Trisaccharide
  • Made up of glucose, galactose, and fructose
  • Galactose in an a-1,6 linkage to a sucrose
48
Q

Inulin

A
  • Energy storage
  • Oligosaccharide
  • Made up of fructose with glucose caps
49
Q

Polysaccharide: Amylose

A
  • Energy storage
  • Made up of several thousands glucose monomers
  • a-1,4 linkage
50
Q

Polysaccharide: Amylopectin

A
  • Energy storage
  • Made up of thousands to hundred thousands of glucose polymers
  • a-1,4 linkage with a-1,6 linkage branched point at every 24-30 residues
51
Q

Polysaccharide: Glycogen

A
  • Energy storage
  • Made up of ten thousands glucose polymers
  • a-1-4 linkage with high a-1,6 branched linkage every 6-12 residues
52
Q

Polysaccharide: Starch

A
  • Plant Energy storage
  • Similar to Glycogen
53
Q

Polysaccharide: Cellulose

A
  • Structural
  • Linear polymers of hundreds to thousands glucose monomers
  • B-1,4 linkage
54
Q

Polysaccharide: Chitin

A
  • Structural
  • B-1,4 linkage of N-Acetylglucosamine
55
Q

Polysaccharide: Alginate

A
  • Structural
  • Copolymer of mannose and glucaronate
56
Q

Energy Storage polysaccharide

A
  • Can be linear or branching
  • Typically has a a-1,6 linkage (branching)
57
Q

Structure polysaccharide

A
  • Linear for structural purposes
  • Typically has a B-1,4 linkage (linear)
58
Q

The 3 control points in glycolysis

A

Step 1, 3, and 10 (committed irreversible steps)
Note: step 3 is considered the first committed stage as step 1 can lead to other pathway

59
Q

Input and Output of Glycolysis

A

Input: 2 ATP, Glucose, 1 NAD+
Output: 4 ATP total (2 Net), 2 Pyruvate, 1 NADH

60
Q

The 2 control points in glucogenesis

A

Step 1 and 2

61
Q

Fatty Acids

A
  • Amphipathic
  • Even number of carbon atoms
  • Insulate and cushion vitals
  • Components of neutral lipids, phospholipids, and eicosanoids
  • Generally found as esters and amides (as it is more stable)
62
Q

Saturated Fatty Acids

A
  • Do not contain double bond
  • Solid at room temperature
  • Unhealthy
63
Q

Unsaturated Fatty Acids

A
  • Contain double bond
  • Liquid at room temperature
  • Monounsaturated: only one double bond
  • Polyunsaturated: has multiple double bond
  • Cis (same direction): Naturally occurring fatty acids
  • Trans (different direction): Hydrogenated fatty acids
64
Q

18:1 delta 9 (w9)

A
  • 18 number of carbons
  • 1 number of double bonds
  • 9 the position of the double bond from the carboxylic acid end
  • w9 the position of unsaturated bond from the omega end (away from carboxylic acid)
65
Q

Neutral Lipids

A

Classification of fatty acids that do have a charged groups as the carboxylic acid is esterified to either glycerol or cholesterol. Allows for safe storage due to the detergent nature of charged groups.

66
Q

Triglycerides

A
  • How we store lipids
  • Unsaturated acid in a triacylglycerol (TAG) is attached to the carbon 2 in the glycerol
  • TAG rarely repeats a fatty acid
  • To mobilize TAGs, we require cholesterol
67
Q

Cholesterol Esters

A
  • Fatty acids esterified to cholesterol
  • Can be stored in the body as a cholesterol reserve
68
Q

Steroids

A
  • Groups of lipids with diverse functions but a common skeleton consisting of four fused rings
  • Made from cholesterol
69
Q

Cholesterol

A
  • Maintains membrane fluidity
  • Transport across the membrane
  • Diffusion of proteins within the membrane
  • Membrane integrity
70
Q

Bile Salt

A

Detergents synthesized from cholesterol by the liver and stored in the gall bladder.

71
Q

Waxes

A

Hydrophobic, long-chain fatty acids esterified to a long chain alcohol

72
Q

Micelle

A

Spherical sphere composed of aggregates of fatty acids at high concentration
Illustration of hydrophobic effect

73
Q

Phospholipids

A

Amphipathic lipid molecules which makes up the main structural components of membranes.
Divided into: glycerophosholipids and sphingolipids

74
Q

Glycerophosholipids

A

Lipid containing glycerol head, two fatty acyl chain, and a phosphoalcohol

75
Q

Sphingolipids

A

Lipid containing one fatty acyl chain and a spingosome backbone and a phosphoalcohol.

76
Q

Eicosanoids

A

Molecules derived from 20 carbon polyunsaturated fatty acids
- Signalling molecules
- Regulating functions such as blood pressure, pain, inflammation, and labour/deliver.

BIOL 311: Biochemistry I (1 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions