Enzyme characteristic - common feature Flashcards

1
Q

example of using enzymes for survival

A

firefly and bombardier beetle

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

firefly

A

light

using luciferase

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

bombardier beetle

A

use catalase - eject boil acid

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

example role for enzymes - 6

A
food digestion (pepsin)
blood clotting (thrombin)
pressure (ACE
defence (lysozyme)
breakdown of drugs (cytochrome p450)
routine cell process
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

types of reaction

A

anabolic
catabolic
interconversion

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

anabolic

A

small to large

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

catabolic

A

larger to small

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

interconversion

A

reaction at equilibrium

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

enzyme classification

A

most end in -ase and common name like trypsin
category names
enzyme commission number - 4 digit

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

category names - how it starts

A

start with same part being broken down

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

enzyme commission number

A

class . subclass . sub-subclass . serial

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

6 classes

A
oxidoreductase
transferase
hydrolase
lyase
isomerase
ligase
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

oxiderductase

A

transfer e-

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

transferase

A

transfer chemical groups like methyl

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

hydrolase

A

break bond with water

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

lyases

A

involve double bond

17
Q

isomerase

A

transfer of group in molecule

two different substrate modify single molecules

18
Q

ligase

A

form bonds using ATP

19
Q

enzyme necessary - pace of life

A

2H2O2 -> 2H2O + O2 - H2O2 is dangerous and requires 41 years to remove
therefore using catalase enzyme - 1s to break down

20
Q

enzyme necessary - condition of life - temp and pH

A

body temp 37 degrees and 7pH

increase rate - increase temp and pH which destroy cell but enzyme - no high temp needed

21
Q

rate of reaction depend on

A

speed of 1 reaction - rate constant

number of reaction happening simultaneously

22
Q

enzyme in reaction

A

reduces activation energy

23
Q

how energy relate to speed - distribution, Ea

A

uneven distribution of energy
enzyme shifts Ea to left therefore more molecules undergo reaction
each has Ea of 5KJ/mol = 10x faster

24
Q

enzyme potency

A

how many times faster with enzyme

e.g. OMP decarboxylase from 78 million yrs to 18ms therefore rate is 10(17)

25
enzyme properties
reusable - save resources specific - only desired reaction efficient - 100% yield of product controllable - start/stop reaction
26
active site properties
small part of enzyme contain binding site and catalytic residue source of substrate - range of substrate - all have that group therefore enzyme specificity provide alternative route that requires less energy
27
lock and key (fischer)
size / shape filter | bind affinity - substrate bind to E
28
induced fact (koshland)
loose and approximate, bind and changes to correct shape | charge in active site and substrate - attract opposite charge
29
stereo-specificity
characterise enzymes | Ogston 3-point binding
30
Ogston 3-point binding
active site has 3 points to have stereospecificity
31
stereospecificity determined by
3D arrangement of residues its chemical properties form catalytic triad
32
catalytic triade
only 3 a.a carefully positioned in actual catalysis
33
active site also contains
metal cofactor coenzyme prosthetic groups
34
metal cofactor
small, dense +ve charge | breaks groups like phosphate group using Mg2+ or Zn2+
35
coenzyme
organic molecule - provide/remove groups derived by vitamins act as H shuttle in Redox reaction no. coenzyme remains same - moving H around
36
example of coenzyme
NADH -> NAD+ - H transferred to S and leaves as P
37
prosthetic groups
e.g. Flavin, Haem (catalase) organic and quite large post translationally modified protein and also metals as well