Biochem Exam 2

Front 1

What are the 6 classes of enzymes?

Back 1

1. Hydrolysis (break bonds by adding H2O) - A-B +H2O -->H-A + B -OH
2. Lysase (create or break bonds)
3. Ligase (create bonds) -
4. Transferase (transfer group) - A-X + B -->A +B-X
5. Isomerase (change structural arrangement)
6. oxidoreductase (redox reactions)

Front 2

Examples of transferases

Back 2

Kinases, methyltransferases

Front 3

Hexokinase

Back 3

phosphorylates glucose-->glucose-6-phosphate

Front 4

Example of hydrolase

Back 4

serine protease, ribonuclease

Front 5

Serine protease. Function and types

Back 5

hydrolyze peptide bonds to cleave aa's

Thrombin: cleaves Arg-Gly in fibrinogen to make fibrin
Trypsin: Cleaves on C terminus of Arg and Lys (basic)

Front 6

RNAse A Mechanisms

Back 6

Uses 2 histidines, one of which is protonated
(His 12 is base His 119 is acid)

Front 7

Why is h2O used in hydrolysis

Back 7

to regenerate the original enzymes

Front 8

Types of isomerases

Back 8

Racemase (L--D), Pin1 prolyl isomerase

Front 9

Pin1 prolyl isomerase

Back 9

switches proline b/w cis and trans, which can act as a regulatory switch

Front 10

LIgases function and exs

Back 10

Ligase=joining of two molecules, using ATP hydrolysis

Ex. tRNA synthase.

Front 11

tRNA synthase.

Back 11

First conerts aa-->high energy aa (aa+ATP-->aa-AMP + PPi)
then high energy aa binds to tRNA (aa-AMP+tRNA-->aa-tRNA+AMP)

Front 12

lysases and ex.

Back 12

can add groups across double bonds to break them.
ex. pyruvate decarboxylase

Front 13

pyruvate decarboxylase

Back 13

pyruvate +pyruvate decarboxylase-->acid aldehyde

Front 14

Exs of oxidoreductase

Back 14

catalase (breaks up h2o2) and alcohol dehydrogenase

Front 15

acid dehydrogenase

Back 15

removes hydrogen from ethyl alcohol with NAD+

Front 16

5 ways to increase rate

Back 16

1. proximity
2. orientation
3. induced fit
4. transition-state stabilization
5. reactive chemical groups

Front 17

number 1 protein tool

Back 17

site-directed mutagenesis

Front 18

onconase

Back 18

same function as rnase but no affinity for the inhibitor, so lethal in the cell

Front 19

zymogen

Back 19

can be formed as pecursors

Front 20

lactate dehydrogenase

Back 20

pyruvate-->lactic acid

tetramer with varying concentrations of LDHA (forward reaction) and LDHB (backward reaction)

Front 21

proinsulin/insulin

Back 21

can only fold correctly in proinsulin phase. won't work in anfinson experiment

Front 22

proteolytic mapping

Back 22

use proteases to cleave protein and compare bands in electrophoresis

Front 23

farnesylation

Back 23

sends proteins to the membrane

Front 24

ubiquinine

Back 24

says "degrade me"

Front 25

which residues get modified

Back 25

phosphorylation on oh residues. lycine gets ubiquinone

Front 26

covalent modifiers

Back 26

kinase and phosphatase

Front 27

Src kinase

Back 27

important for cancer. if phosphorylated, inactive. cancer cells can't be phosphorylzed and continue to grow

Front 28

types of lipids

Back 28

phopsholipids
glycosphingolipids
isoprenoids

Front 29

major component of membrane

Back 29

glycerophospholipids

Front 30

pyruvate kinase

Back 30

coupled with adp->atp with PEP-->pyruvate