Biotech Test 1 Set 1

Front 1

Biotechnology def. (3)

Back 1

use of:
1)MOs
2)living cells
3)animals
to produce useful pharmaceuticals

Front 2

IMPACT of Biotechnology (3)

Back 2

1)sequencing of human genome has led to novel therapeutics
2)improvement of patient's reponse to treatment
3)great impact on chronic disease but mostly treat acute treatments

Front 3

Biotech methods of making novel medical agents (6)

Back 3

1)recombiant DNA
2)hybridoma
3)transgenic technology (pharming)
4)nuclear transfer technology
5)Antisense therapy
6)gene therapy

Front 4

___ is one of the fastest enzymes known

Back 4

carbonic anhydrase

Front 5

Properties of enzymes (2)

Back 5

1)enzymes have immense catalytic power
2)highly specific (stereospecific and geometric specific)

Front 6

Enzymes catalyze...

Back 6

a single chemical rxn or a set of closely related rxns

Front 7

Much of the catalytic power of an enzymes comes from

Back 7

binding substrates in favorable orientation in ES complexes

Front 8

Catalytic specificity depends on...

Back 8

specificity of binding

Front 9

Catalytic groups?

Back 9

residues that directly participate in the making and breaking of bonds

Front 10

Active Site key features (5)

Back 10

1)clefts/crevices
2)small part of total enzyme volume
3)3D entity formed by groups that come from different parts of the AA sequence
4)substate bound to AS by multiple weak reversible interactions
5)specificity of binding which depends on arrangement of atoms in AS

Front 11

Types of weak reversible interactions used in the AS? (3)

Back 11

1)hydrophobic
2)ionic
3)hydrogen bonding

Front 12

2 models for ES binding interaction

Back 12

1)lock and key
2)induced fit

Front 13

Induced Fit?

Back 13

enzyme changes shape to more tightly bind substrate after initial binding

Front 14

Enzyme inhibitors?

Back 14

substance that can decrease the enzyme activity

Front 15

2 types of enzyme inhibition?

Back 15

irrerversible inhibition
reversible inhibition

Front 16

2 types of REVERSIBLE inhibition?

Back 16

1)competitive inhibition
2)non-competitive inhibition

Front 17

Irreversible inhibition? and 2 Ex (and what do they inhibit)

Back 17

when inhibitor forms a covalent bond with the enzyme

Aspirin (COX)
Penicillin (transpeptidase)

Front 18

Competitive inhibition (3)

Back 18

1)inhibitors compete for AS w/ the normal substrate
2)inhibitor must have similar structure to natural substrate
3)success of inhibitor binding depends on [] compared to substrate []

Front 19

Why is competitive inhibtion reversible?

Back 19

b/c whether or not the inhibitor binds to AS depends on its [] relative to the normal substrates []

Front 20

Non-competitive inhibitor?

Back 20

reduce enzyme activity by distorting the enzyme by binding to some other ALLOSTERIC site

Front 21

Non-competitive inhibition reversible?

Back 21

yes if the inhibitor [] is diminished (and binding is non-covalent)

Front 22

Classes of enzymes (6)

Back 22

1)oxioreductases
2)transferases
3)hydrolases
4)lyases
5)isomerases
6)ligases

Front 23

Basic desc of oxioreductases

Back 23

catalyzes oxidation reduction of substrates

Front 24

Basic desc of transferases

Back 24

transfer groups b/w substrates

Front 25

Basic desc of hydrolases

Back 25

catalyze hydrolysis via
1)esterases
2)carbohydrases
3)proteases
4)amidases

Front 26

Basic desc of lyases

Back 26

catalyze removal of -OH groups and leave double bonds

Front 27

Basic desc of isomerases

Back 27

catalyze conversion of one isomer to another

Front 28

Basic desc of ligases

Back 28

catalyze linking of 2 substrates together

Front 29

Hydrolases catalyze hydrolysis of....bonds (4)

Back 29

1)ester (in fats)
2)glycosidic
3)peptide
4)amide

Front 30

Carbohydrases hydrolyze what type of bond

Back 30

glycosidic

Front 31

Amylase rxn

Back 31

starch to glucose

Front 32

Sucrase rxn

Back 32

sugar to glucose and fructose

Front 33

Lactase rxn

Back 33

Lactose to glucose and galactose

Front 34

Ligase fxn and example

Back 34

link two substance by using ATP

DNA ligase forms phosphodiester bonds

Front 35

____ is an ENZYMATIC drug that is used to treat Cystic Fibrosis

Back 35

Pancreatin

Front 36

Pancreatin
a)is used as a....
b)what is special about dosage form?
c)used to treat...(2)

Back 36

a)digestive aid
b)it is enteric coated so the stomach doesn't denature the enzyme
c)ppl with pancreatic deficiencies and CF

Front 37

Pancreatin
a)contains...
b)obtained from...

Back 37

a)proteases, lipase, amylase
b)pancreas of hogs and ox

Front 38

Pancreatin
a)contains...(in mg)(3)
b)usual dose and sig
c)brand names (3)

Back 38

a)25mg protease, 25mg amylase, 2mg lipase
b)325mg to 1g before meals
c)Viokase, Panteric, Elzyme

Front 39

Pancrelipase
a)contains...
b)is essentially...
c)each mg contains...

Back 39

a)lipase, amylase, proteases
b)more []ed form of pancreatin
c)24units lipase, 100units amylase, 100units protease

Front 40

Pancrelipase []s vs. Pancreatin []s

Back 40

12x increase in lipase

4x increase in amylase/protease

Front 41

Pancrelipase
a)fxn
b)brand names(2)

Back 41

a)digestive aid, CF
b)Pancrease, Creon

Front 42

Thrombolytics lysis of the clot is regulated by..

Back 42

fibrinolytic system

Front 43

....(2) are what a clot is made of

Back 43

fibron
platelets

Front 44

Early thrombolytic therapy is very benefical for what condition?

Back 44

MI

Front 45

t-PA fxn (2)

Back 45

converts inactive Plasminogen to active Plasmin

is clot specific, once it binds to clot its activity goes up 600x

Front 46

Plasmin?

Back 46

proteolytic to fibrin

Front 47

Having too much plasmin in your system can result in...

Back 47

cerebral hemmoraging

Front 48

Streptokinase
a)fxn
b)got from...
c)type of enzyme

Back 48

a)plasminogen activator like t-PA
b)cultures of group C hemolytic streptococci
c)TRANSFERASE not protease

Front 49

Streptokinase
a)mechanism (2)

Back 49

a)activates plasminogen indirectly by transferring a phosphate group from ATP to the serine residue in buried AS of plasminogen
2)phosphorylation alters its conformation exposing the buried AS of the plasminogen

Front 50

Streptokinase disadvantages (4)

Back 50

1)foreign bacterial protein so can have allergic rxns
2)fever
3)resistance via previous infection by streptoccal or previous therapy w/ the drug
4)cerebral bleeding

Front 51

APSAC (anisolyated plasminogen streptokinase activator complex) def.

Back 51

anisoyl derivative of the active site of the plasminogen component of the complex

Front 52

APSAC (anisolyated plasminogen streptokinase activator complex) mechanism (3)

Back 52

1)acylation of lysine inactivates the plasminogen's AS but it does NOT decrease the affinity of the complex for fibrin
2)resultant slow deaceylation of lysine upon binding of the complex to the fibrin of the clot leads to activation of the plasminogen
3)fibrinolysis of clot

Front 53

APSAC
a)shortcomings are...
b)advantage

Back 53

a)SAME AS streptokinase
b)increased half-life over streptokinase

Front 54

Urokinase
a)source
b)type of enzyme
c)mechanism

Back 54

a)human urine/kidney cells
b)TRANSFERASE
c)activates plasminogen SAME WAY as streptokinase

Front 55

Urokinase advantages (2)

Back 55

1)is human protein so doesn't cause allergy like streptokinase
2)good for streptokinase resistant/allergic patients

Front 56

Secondary protein structure
a)def (2)
b)2 main

Back 56

a)regions of ordered structure taken by the protein due to AAs near to one another in a linear sequence (involves H-bonds)
b)alpha helix, beta sheet

Front 57

Alpha helix
a)def.
b)maintained by...

Back 57

results from coiling of protein so that peptide bond making up the backbone form hydrogen bonds
b)H-bonds b/w C=O and N-H of every 4th peptide

Front 58

Beta sheet def. (2)

Back 58

a)layering of protein chains, one on top of another
b)held together by hydrogen bonds b/w peptide bonds of adjacent polypeptide chains

Front 59

Tertiary protein strucute
a)def.
b)maintained by...(2)

Back 59

a)3D shape of protein
b1)series of noncovalent bonds b/w side chains on polypeptide chain
b2)bonds are b/w DISTANT AAs

Front 60

Tertiary structure
a)vital for...
b)of enzymes/receptors is crucial for...

Back 60

a)protein fxn
b)fxn and interaction w/ drugs

Front 61

Quaternary protein structure
a)def.

Back 61

a)spatial arrangements of subunit, interaxn of multiple proteins

Front 62

What type of bonding is most important to Quaternary Structure? but what other bonds are involved

Back 62

IONIC

hydrophobic bonds

Front 63

What happens if HYDROPHOBIC bonds are on surface of protein? (regarding Quaternary Structure)

Back 63

interaxn of 2 protein subunits and formation of dimer

Front 64

2 diseases caused by genetic mutations

Back 64

1)Sickle cell disease
2)cystic fibrosis