General Biochemistry

Front 1

Contain a hydrocarbon tail and a polar carboxylate head.

Back 1

fatty acids

Front 2

Lipid: composed of 3 fatty acyl recidues esterified to a glycerol.

Back 2

triacylglycerols (TAGs)

Front 3

Lipid: possess a glycerol backbone, with 2 fatty acids and a phosphate group.

Back 3

glycerophospholipids

Front 4

Lipid: contain a spingosine head which is similar to a glycerol backbone, two nonpolar tails and a polar headgroup.

Back 4

spingolipids

Front 5

Contain four fused rings, 3 6-carbon rings and one 5-carbon ring.

Back 5

steroids

Front 6

In the membrane, spingolipids point towards which side?

Back 6

extracellular leaflet

Front 7

In the membrane, glycerophospholipids point towards which side?

Back 7

cytosolic leaflet

Front 8

Membrane protein: usually span the bilayer, may have polar residues in the interior for passage of polar molecules and ions.

Back 8

integral membrane proteins

Front 9

Membrane protein: associated with membrane face through charge-charge or H-bonding interactions to integral proteins and membrane lipids. More readily dissociated from membrane.

Back 9

peripheral membrane proteins

Front 10

Membrane protein: tethered to membrane through a protein-lipid covalent bond.

Back 10

Lipid-anchored membrane proteins

Front 11

Catalyze redox reactions.

Back 11

oxidoreductases

Front 12

Catalyze group transfer reactions.

Back 12

transferases

Front 13

Cleave a bond with the addition of water.

Back 13

hydrolases

Front 14

Catalyze cleavage of a substrate by cleaving a bond and leaving a double bond.

Back 14

lyases

Front 15

Catalyse isomerism reactions.

Back 15

isomerases

Front 16

Catalyze ligation of two substrates.

Back 16

ligases

Front 17

Active site fits better to substrate after binding.

Back 17

induced fit

Front 18

Substrate and inhibitor bind to the same site, inhibitor binds only to free enzyme.

Back 18

competitive inhibition

Front 19

In competitive inhibition, what happens to Vmax and Km?

Back 19

Vmax stays the same and Km increases.

Front 20

Inhibitor binds to a different site on the enzyme or to the enzyme-substrate complex, affects enzyme shape.

Back 20

noncompetitive inhibition

Front 21

In noncompetitive inhibition, what happens to the rate if substrate is added?

Back 21

rate is not restored

Front 22

Inhibitor binds only to the enzyme-substrate complex, only occurs with multisubstrate enzymes.

Back 22

uncompetitive inhibition

Front 23

Where do allosteric inhibitors/activators bind on an allosteric enzyme?

Back 23

a secondary regulatory site different from the active site.

Front 24

Kinetic plots for an allosteric enzyme are what shape?

Back 24

sigmoidal

Front 25

What centrifugal force would you use to separate mitochondria and chloropolasts?

Back 25

3000-5000 G

Front 26

If a protein solution's pH is less than pI (pH < pI), the protein will move to which side?

Back 26

positive

Front 27

If a protein solution's pH is greater than its pI, the protein will move to which side?

Back 27

negative

Front 28

Many antibodies recognizing different epitopes on the same antigen.

Back 28

polyclonal

Front 29

One antibody recognizing the same epitope on the antigen.

Back 29

monoclonal

Front 30

Rotation allowed around the N-Ca in an amino acid is denoted by?

Back 30

phi

Front 31

Rotation allowed around the Ca-C in an amino acid is denoted by?

Back 31

psi

Front 32

The semi-stable intermediate state of a protein.

Back 32

molten globular state

Front 33

The biggest driving force for protein folding.

Back 33

increase in entropy from the displacement of water

Front 34

Class of molecular chaperone: small, aggregates around unfolded proteins to assist in folding and preventing them from aggregating.

Back 34

Hsp70

Front 35

Molecular chaperone: has a large lumen where an unfolded protein enters and emerges as a folded protein.

Back 35

Hsp60

Front 36

Breakdown of metabolites.

Back 36

catabolism

Front 37

Buildup of metabolites.

Back 37

anabolism

Front 38

Metabolite early in the pathway activates an enzyme further down the pathway.

Back 38

feed-forward activation

Front 39

Short term compound for energy storage.

Back 39

ATP

Front 40

Produces a high energy thioester linkage when coupled to acetate.

Back 40

acetyl coA

Front 41

Energy can also be stored as reduced coenzymes such as?

Back 41

NADH, FADH2, QH2

Front 42

Conversion of 1 glucose to 2 pyruvate.

Back 42

glycolysis

Front 43

Net energy generation of glycolysis.

Back 43

2 ATP, 2 NADH

Front 44

Step 1 in GLYCOLYSIS, include enzymes.

Back 44

glucose --> glucose 6-phosphate

by hexokinase, glucokinase

Transfer of a phosphoryl group from ATP to glucose.

Front 45

Step 2: GLYCOLYSIS, include enzymes.

Back 45

Glucose 6-phosphate --> fructose 6-phosphate

by glucose 6-phosphate isomerase

Isomerization

Front 46

Step 3: GLYCOLYSIS, include enzymes.

Back 46

Fructose 6-phosphate --> fructose 1,6-bisphosphate

by: phosphofructokinase-1

Transfer of second phosphoryl group from ATP.

Front 47

Step 4: GLYCOLYSIS, include enzymes.

Back 47

Fructose 1,6-bisphosphate <--> glyceraldehyde-3-phosphate <--> dihydroxyacetone phosphate

by: aldolase

Splitting of fructose and rapid interconversion of triose phosphates.

Front 48

Step 5: GLYCOLYSIS

Back 48

Glyceraldehyde-3 phosphate <--> 1,3-bisphosphoglycerate

by: glyceraldehyde 3-phosphate dehydrogenase

OXIDATION and PHOSPHORYLATION.

NADH produced

Front 49

Step 6: GLYCOLYSIS

Back 49

1,3-bisphosphoglycerate <--> 3-phosphoglycerate

by: phosphoglycerate kinase

Transfer of Pi to ADP.

ATP produced.

Front 50

Step 7: GLYCOLYSIS

Back 50

3-phosphoglycerate <--> 2-phosphoglycerate

by: phosphoglycerate mutase

Isomerization.

Front 51

Step 8: GLYCOLYSIS

Back 51

2-phosphoglycerate <--> phosphoenolpyruvate

by: enolase

Reorganization

Front 52

Step 9: GLYCOLYSIS

Back 52

Phosphoenolpyruvate --> pyruvate

by: pyruvate kinase

Transfer of Pi to ADP.

ATP produced.

Front 53

In anaerobic conditions, pyruvate is converted to this.

Back 53

ethanol

Front 54

In aerobic conditions, pyruvate is converted to this.

Back 54

acetyl CoA

Front 55

Regulation of phosphofructokinase-1 (PFK-1)

Back 55

-ATP inhibits PFK-1.
-AMP activates PFK-1 by relieving ATP inhibition.
-Elevated citrate also inhibits PFK-1.

-Activated by fructose-2,6-bisphosphate

Front 56

Regulation of hexokinase.

Back 56

-Glucose-6-phosphate (G6P) from step 1 inhibits hexokinase (feedback inhibition).

Front 57

Regulation of pyruvate kinase.

Back 57

-ATP inhibits pyruvate kinase
- also inhibited by PKA
- activated by fructose 1,6-bisphosphate

Front 58

Other sugars that can enter glycolysis.

Back 58

Fructose: --> glyceraldehyde-3-phosphate

Galactose: --> glucose 6-phosphate

Mannose: converted to fructose 6-phosphate