Brainscape's Knowledge GenomeTM


Top Flashcards (Certified)
All Flashcards

Biochem > Quan SG > Flashcards

Quan SG Flashcards

(82 cards)

Start Studying
1
Q

a catalysts of biological reactions

A

Enzymes

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

what type of rxns do enzymes catalyze

A

thermodynamically possible

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

are enzymes used or changed during the rxn?

A

No

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

Do enzymes change the equilibrium or direction during the rxn?

A

No

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

what is the optimal temperature for most enzymes

A

37 C

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

every enzyme has its own optimal …

A

temperature & pH

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

what is trypsin’s optimal pH?

A

6-7

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

what is pepsin’s optimal pH?

A

2-3

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

because of the effect of pH on the ionic charge of AA side chains of an enzyme results in …

A

pH sensitivity

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

what kind of enzymes catalyze oxidation-reduction rxns

A

Oxidoreductases

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

what kind of enzymes catalyze group transfer rxns

A

Transferases

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

what kind of enzymes catalyze hydrolysis rxns where water is acceptor of transferred group

A

Hydrolases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

what kind of enzymes catalyze lysis of a substrate, generating a double bond in a non-hydrolytic, non-oxidative elimination

A

Lysases (synthase)

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

what kid of enzymes catalyze isomerization rxns

A

Isomerases

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

what kind of enzymes catalyze ligation, or joining of 2 substrates

A

Ligases (synthase)

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

what kind of enzyme requires ATP?

A

Ligases (synthase)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

what contains the function groups of the enzyme?

A

Active site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

specific region in an enzyme to which substrate molecule is bound

A

Active site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

at what part of the enzyme does the catalytic active occur?

A

Active site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

what part of the enzyme contains the the functional group?

A

Active site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

how do enzymes bind to substrates?

A

weak, non-covalent bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

the theory that an active site of an enzymes only accepts a specific substrate

A

Lock & Key (Fischer theory)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

one enzyme acts only on one substrate

A

absolute enzyme

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

one enzyme acts on different substrates that all have the same bond type

A

Relative

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
enzymes that catalyze the transformation of only substrates which are in certain geometrical configuration (cis or trans)
Stereospecific
26
One international unit (IU) catalyzes conversion of 1 mol of substrate to product per minute
Enzyme activity
27
the specific activity of an enzyme is a measure of the number of IU/mg protein
Enzyme activity
28
inhibitor has structure similar to the substrate, being able to bind to same active site and prevents binding of substrate
competitive inhibitor
29
How can the activity of a competitive inhibitor be reversed?
by increasing [s]
30
an inhibitor that binds to an enzyme site different from the active site & changes the shape of the enzyme active site so the substrate can no longer bind
Non-competeitive inhibitor
31
this type of inhibition cannot be overcome by increasing [s]
Non-competeitive inhibitor
32
an inhibitor that binds to the enzyme-substrate compels
uncompetitive inhibitor
33
type of inhibition that usually only occurs in multiple substrate rxns
uncompetitive inhibitor
34
what class of inhibitors is non-covalently bound to the enzyme
reversible inhibitors
35
tightly bound through covalent or non-covalent interactions
irreversible inhibitors
36
react with specific R groups of AA’s
Group-specific reagent
37
structurally similar to the substrate for the enzyme and covalently alter active site
Substrate Analogs
38
enzyme participates in its own irreversible inhibition
Suicide Inhibitors
39
bind non-covalently to allosteric site and regulate enzyme activity via conformational changes
allosteric modulators
40
a type of enzyme regulation involving the binding of a non-substrate molecule at locations on the enzyme other than the active site.
allosteric control
41
covalent attachment of a molecule to an AA side chain can modify the enzyme
reversible, covalent modification
42
multiple forms of an enzyme which differ in AA sequence but can catalyze the same reaction
ISOENZYMES (ISOZYMES)
43
many enzymes synthesized as inactive precursors (zymogens) that are activated by
proteolytic cleavage
44
inactive enzyme activated upon cleavage
proteolytic cleavage
45
three examples of proteolytic cleavage enzymes
digestive, blood clotting, and insulin
46
cascade of proteolytic activations is used in what pathway
blood clotting
47
synthesized as zymogens in stomach and pancreas
digestive enzymes
48
proinsulin to insulin by removal of a peptide
proteolytic cleave, protein hormones
49
glycolysis turns glucose into what
lactate
50
ATP, glycogen, ribose, lipid molecules, and NADPH can be generated from
glucose
51
stored in the cell as Glc-6-P
glucose
52
what is the rate limiting step of glycolysis?
PFK-1
53
Net gain of ATP from glycolysis?
4ATP - 2ATP = 2ATP
54
pyruvate can be transformed to ______ to regenerate NAD+
lactate
55
pyruvate + NADH2 --> lactate + NAD+
LACTATE DH RXN
56
pyruvate + NADH2 --> lactate + NAD+ is catalyzed by
lactate DH
57
glucose + ATP --> G6P + ADP | is catalyzed by
Hexokinase
58
Hexokinase is inhibited by
G6P
59
Pentose phosphate pathway is important for the generation of
NADPH and Ribose
60
what is used as the building block for glycogen?
UDP-glucose
61
used as immediate precursor for glycogen synthesis
UDP-glucose
62
catalyzes elongation of chains glycogen is initiated by
glycogen synthase (glycogenin)
63
catalyzes attachment of glucose molecule to one of its own tyrosine residues
glycogenin
64
a type of covalent bond that joins anomeric C1 of a glucose molecule and OH of tyrosine side chain of glycogenin
glyosidic bond
65
catalyzes phospohrolytic cleavage of 1-4 glycosidic linkages of glycogen, releasing G1P as rxn product
GLYCOGEN PHOSPHORYLASE
66
glycogen (n residues) + Pi -> glycogen (n-1 resides) + G-1-P
GLYCOGEN PHOSPHORYLASE
67
stimulated by Epinephrine and Glucagon
GLYCOGEN PHOSPHORYLASE
68
Inhibition of glycogen phosphorylase can be used to treat what?
Diabetes
69
inhibitors bind at the dimer interface, stabilizing the inactive (tense) conformation of GP
glycogen phosphorylase inhibition for treatment of diabetes
70
almost the reverse of glycolysis
Gluconeogenesis
71
3 IRREVERSIBLE STEPS OF GLYCOLYSIS THAT MUST BE BYPASSED IN GLUCONEOGENSIS
Hexokinase Phosphofructokinase Pyruvate Kinase
72
triggered by the hormone glucagon when blood glucose is low
Glucagon-cAMP cascade in the liver
73
inhibition of glycolysis and glycogen synthesis is the result of?
Glucagon-cAMP cascade in the liver
74
stimulation of gluconeogenesis and glycogen breakdown | free glucose is formed for release to the blood is the result of?
Glucagon-cAMP cascade in the liver
75
Cycle used during muscle exercising
Cori cycle
76
Lactate produced from pyruvate passes via the blood to the liver, where it may be converted to glucose through gluconeogensis
Cori cycle
77
the glucose released into the blood to travel back to the muscle to fuel glycolysis by what cycle
cori, during exercise
78
costs 6~P in liver for ever 2~P made available in muscle (net 4~P)
cori cycle
79
Where does TCA cycle occur
Mitochondrial matrix
80
is derived from pyruvate via pyruvate carboxylase (1st step in gluconeogenesis)
oxaloacetate
81
is derived from pyruvate. via PDH complex
Acetyl-CoA
82
Pyruvate dehydrogenase catalyze the synthesis of
Acetyl-CoA

Biochem (2 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions