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
Q

enzyme properties

A

reusable - save resources
specific - only desired reaction
efficient - 100% yield of product
controllable - start/stop reaction

26
Q

active site properties

A

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
Q

lock and key (fischer)

A

size / shape filter

bind affinity - substrate bind to E

28
Q

induced fact (koshland)

A

loose and approximate, bind and changes to correct shape

charge in active site and substrate - attract opposite charge

29
Q

stereo-specificity

A

characterise enzymes

Ogston 3-point binding

30
Q

Ogston 3-point binding

A

active site has 3 points to have stereospecificity

31
Q

stereospecificity determined by

A

3D arrangement of residues
its chemical properties
form catalytic triad

32
Q

catalytic triade

A

only 3 a.a carefully positioned in actual catalysis

33
Q

active site also contains

A

metal cofactor
coenzyme
prosthetic groups

34
Q

metal cofactor

A

small, dense +ve charge

breaks groups like phosphate group using Mg2+ or Zn2+

35
Q

coenzyme

A

organic molecule - provide/remove groups
derived by vitamins
act as H shuttle in Redox reaction
no. coenzyme remains same - moving H around

36
Q

example of coenzyme

A

NADH -> NAD+ - H transferred to S and leaves as P

37
Q

prosthetic groups

A

e.g. Flavin, Haem (catalase)
organic and quite large
post translationally modified protein and also metals as well