Honors Bio

0.0(0)
studied byStudied by 0 people
GameKnowt Play
learnLearn
examPractice Test
spaced repetitionSpaced Repetition
heart puzzleMatch
flashcardsFlashcards
Card Sorting

1/95

encourage image

There's no tags or description

Looks like no tags are added yet.

Study Analytics
Name
Mastery
Learn
Test
Matching
Spaced

No study sessions yet.

96 Terms

1
New cards
2
New cards
3
New cards
4
New cards
5
New cards
Enzyme Study Guide
6
New cards
🔹 What Are Enzymes?
7
New cards
Enzymes are proteins that act as biological catalysts → they speed up reactions without being used up.
8
New cards
9
New cards
10
New cards
Found in almost all living organisms.
11
New cards
12
New cards
13
New cards
Humans use enzymes to break down biomolecules in digestion.
14
New cards
15
New cards
16
New cards
Excretory, digestive, and circulatory systems all use enzymes.
17
New cards
18
New cards
19
New cards
🔹 Types of Digestive Enzymes
20
New cards
Amylase → breaks down starch/carbohydrates into glucose.
21
New cards
22
New cards
23
New cards
Lipase → breaks down fats (in the small intestine).
24
New cards
25
New cards
26
New cards
Pepsin & Trypsin → break down proteins (in the stomach and small intestine).
27
New cards
28
New cards
29
New cards
Nucleases → break down nucleic acids (DNA/RNA) into nucleotides.
30
New cards
31
New cards
32
New cards
🔹 Active Site & Substrate
33
New cards
Active site = specific region on the enzyme where the substrate binds.
34
New cards
35
New cards
36
New cards
The substrate must fit perfectly in the active site (like lock & key).
37
New cards
38
New cards
39
New cards
Induced fit = enzyme slightly changes its shape to better hold the substrate after binding.
40
New cards
41
New cards
🔹 Cofactors & Coenzymes
42
New cards
Cofactors = usually inorganic (like metal ions).
43
New cards
44
New cards
45
New cards
Coenzymes = usually organic (often vitamins).
46
New cards
47
New cards
48
New cards
Both often bind at the enzyme’s active site to help the enzyme work.
49
New cards
50
New cards
51
New cards
🔹 Enzyme Inhibition
52
New cards
Competitive inhibitor → sits in the active site, blocking the substrate.
53
New cards
54
New cards
55
New cards
Allosteric inhibitor (non-competitive) → binds at a different site, causing the active site to change shape so the substrate can’t bind.
56
New cards
57
New cards
58
New cards
Main effect of inhibitors = slow down or stop enzyme activity.
59
New cards
60
New cards
61
New cards
Feedback inhibition → cells stop producing excess products (saves energy/resources).
62
New cards
63
New cards
64
New cards
Example: Penicillin kills bacteria by blocking enzymes that help build bacterial cell walls.
65
New cards
66
New cards
67
New cards
🔹 Catalase Example
68
New cards
Catalase enzymes break down hydrogen peroxide (H₂O₂) into water (H₂O) + oxygen (O₂).
69
New cards
70
New cards
71
New cards
Catalase works extremely fast.
72
New cards
73
New cards
74
New cards
Substrate = hydrogen peroxide.
75
New cards
76
New cards
77
New cards
Products = oxygen + water.
78
New cards
79
New cards
🔹 How Enzymes Speed Reactions
80
New cards
They lower activation energy needed for a reaction.
81
New cards
82
New cards
83
New cards
Make reactions more likely/spontaneous by pulling/tugging on bonds in substrates.
84
New cards
85
New cards
86
New cards
🔹 Factors Affecting Enzyme Activity
87
New cards
Temperature & pH matter because enzymes are proteins, and protein structure is sensitive.
88
New cards
89
New cards
90
New cards
Each enzyme has an optimal temperature and pH.
91
New cards
92
New cards
93
New cards
On a graph → the “peak” is the optimal condition.
94
New cards
95
New cards
96
New cards
Denatured = protein shape changes permanently (enzyme stops working).