Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

AGBI 410 > Lecture 29-30 > Flashcards

Lecture 29-30 Flashcards

1
Q

do plants use amino cids for energy

A

no

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

how do plants get nitrogen

A

nitrogen fixing bacteria (N2 to NH3)

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

where does degradation occur of dietary proteins

A

gastrointestinal tract

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

hormone secreted when dietary protein enters the stomach

A

gastrin

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

what does gastrin stimulate the release of

A

HCl and pepsinogen

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

zymogen that is converted to active pepsin by autocatalytic cleavage at low pH

A

pepsinogen

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

cleaves long polypeptide chains into a mixture of smaller peptides

A

pepsin

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

hormone secreted into the blood in response to low pH in the small intestine

A

secretin

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

where is secretin secreted

A

into the blood

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

what does secretin stimulate

A

pancreas to secrete carbonate into the small intestine

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

hormone secreted into the blood in response to the arrival of peptides in the duodenum

A

choleccystokinin

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

zymogens are secreted by what

A

exocrine cells of the pancreas

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

what does cholecystokinin stimulate secretion of

A

trypsinogen, chymotrypsinogen, procarboxypeptidase A and B

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

zymogen of trypsin

A

trypsinogen

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

zymogen of chymotrypsin

A

chymotrypsinogen

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

zymogen of carboxpeptidases A and B

A

procarbboxypeptidases A and B

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

proteolytic enzyme that converts trypsinogen to trypsin

A

enteropeptidase

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

eteropeptidase converts what to what

A

trypsinogen to trypsin

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

activates additional trypsinogen, chymotrypsinogen, procarboxypeptidase, and proelastase

A

trypsin

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

protein inhibitor that further protects the pancreas against self digestion

A

pancreatic trypsin inhibitor

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

what is the first thing to break down proteins

A

pepsin

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

what is used as a marker for protein degradation

A

ubiquitin

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

what are proteins degraded by

A

28S proteasome

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

what is structure of 26S

A

hollow

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

ubiquitin protein enters where

A

26S core,

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

what happens to protein in 26S core

A

is broken to free amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

what are the free amino acids made during protein degradation used for

A

new proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

wehre does most of amino acid catabolism and syn take place

A

liver

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

what amino acids enter liver

A

ones you consume (via blood vessels)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

why can’t ammonia be transported in blood

A

increase in blood pH

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

due to not being able to transport ammonia, what does this mean

A

we cannot just deaminate Amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

how is NH4 transported safely

A

certain amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

first step of transporting NH4

A

transamination

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

what is the accepting amino acid for NH4

A

alpha ketoglutarate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

what is cofactor for transamination

A

vitamin b6

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

transfer alpha amino group to a carbon atom of alpha

A

transamination rxn

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

catalyze the removal of the alpha amino groups

A

aminotransferases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

are transamination reactions irreversible or reversible

A

reversible

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

what does ammonia compete with

A

K+

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

why does ammonia compete with K+

A

for transport into astrocyte cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

1 urea molecule = what

A

2 molecules of nitrogen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

what accepts an amino group

A

PLP (aldehyde form)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

donates its amino group to an alpha keto acid

A

pyridoxamine phosphate (aminated form)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

what does Nh4 and K+ competition result in

A

elevated extracellular (K+)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q

symporter that transports Na, K. Cl

A

Na2+-K+-2Cl- cotransporter 1 (NKCC1)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

excess Cl- from the excess K+ alters what

A

neuronal response to the neurotransmitter GABA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

what transports N from muscle to liver

A

alanine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

what else can be used to transport N

A

glutamine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

how is glutamine made

A

glutamine synthesis, requires ATP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
50
Q

organism that excretes N2 in the form of ammonia

A

ammonotelic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
51
Q

organism that excretes urea

A

ureotelic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
52
Q

organism that excretes uric acid

A

uricotelic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
53
Q

what are the ammonotelic animals

A

most aquatic vertebrates

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
54
Q

uricotelic anomals

A

birds, reptiles

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
55
Q

ureotelic animals

A

many terrestrial vertebrates, also sharks

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
56
Q

glutamate releases its amino group as

A

ammonia in the liver

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
57
Q

NH4+ in the mitochondria comes form many different alpha amino acids in the form of -

A

amino group of l-glutamate, amide nitrogen of glutamine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
58
Q

pathway by which alanine carries ammonia and the carbon skeleton from pyruvate to liver

A

glucose alanine cycle

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
59
Q

catalyzes the oxidative deamincation of glutamate to produce NH4+ and alpha ketoglutarate

A

l-glutamate dehydrogenase

60
Q

where is l-glutamate dehydrogenase present

A

mitochondrial matrix

61
Q

alpha ketoglutartate product can be…

A

oxidized as fuel, or serve as a glucose precursor in gluconeogenesis

62
Q

glutamate dehydrogenase is positively modulated by..

A

ADP (signals low glucose levels)

63
Q

glutamate dehydrogenase dehydrogenase is negatively modulated by..

A

GTP (signals high levels of alpha ketoglutarate)

64
Q

skeletal muscles produce what

A

pyruvate, lactate ammonia

65
Q

interconverts pyruvate and alanine via transamination with glutamate

A

allanine aminotransferase

66
Q

interconverts pyruvate and alanine via transamination with glutamate

A

alanine aminotransferase

67
Q

catalyzes combination of free ammonia with glutamate to yield glutamine

A

glutamate synthetase

68
Q

critical to transport toxic ammonia to liver

A

glutamine synthetase

69
Q

does glutamine synthetase require ATP

A

yes

70
Q

glutaminase

A

catalyzes conversion of glutamine to glutamate and NH4+

71
Q

used to syn other N containing compounds, transport N from extra haptic tissues to liver

A

glutamine

72
Q

is glutamine regulated

A

yes, highly

73
Q

glutamine synthetase is active when

A

deadenylylated

74
Q

glutamine synthetase inactive when

A

adenylylated

75
Q

is AMP on active or inactive version of glutamine synthetase

A

inactive

76
Q

glutamine synthetase converts what to what

A

glutamate to glutamine

77
Q

product of glutamine are…

A

inhibitors of glutamine snthetase

78
Q

adding AMP

A

adenylation

79
Q

glutamate dehydrogenase deaminates what to what

A

Glutamate to alpha keto gluturate

80
Q

glutaaminase deaminates what to what

A

glutamine to glutamate

81
Q

how is uridylylation regulated

A

allosteric regulation

82
Q

where does urea cycle take place

A

cytosol and mitochondria

83
Q

bicarbonate activated by phosphorylation , what enzyme

A

carbamoyl phosphate synthetase 1

84
Q

what does carbamoyl phosphate synthetase 1 switch

A

swaps phosphate for ammonia

85
Q

does Carbamoyl phosphate synthetase 1 use ATP

A

yes

86
Q

how many ATP is required to make a carbamoyl phosphate

A

2

87
Q

urea cycle step 1

A

ornithine + carbamoyl phosphate -> citruline

88
Q

urea cycle step 1 enzyme

A

ornithine transcarbamoylase

89
Q

urea cycle step 2

A

citruline -> argininosuccinate

90
Q

enzyme for step 2

A

argininosuccinate synthetase

91
Q

two cofactors of step 2

A

ATP + aspartate -> PPi + AMP

92
Q

urea cycle step 3

A

argininosuccinate -> arginine

93
Q

what leaves in step 3

A

fumarate

94
Q

step 3 enzyme

A

argininosuccinase

95
Q

step 4

A

arginine -> ornithine

96
Q

enzyme step 4

A

arginase

97
Q

what’s used and released in step 4

A

h2o in, urea out

98
Q

how many amino groups = 1 urea

A

2

99
Q

how many ATP are used for urea cycle

A

2 atp (+2ATP for carbamoyl phosphate)

100
Q

what is the 1 thing you get from urea cycle

A

1 fumarate

101
Q

what can fumarate be converted to

A

malate

102
Q

what can be used to form malate

A

fumarate

103
Q

functions to regenerate NADH in the mitochondria

A

malate aspartate shuttle

104
Q

2 ways urea cycle is regulated

A

level of enzyme synthesis, allosteric regulation of carbamoyl phosphate synthetase 1

105
Q

catalyzes formation of N-acetyl glutamate from acetyl CoA and glutamate

A

N-acetylglutamate synthase

106
Q

allosterically activates carbamoyl phosphate synthetase 1

A

n-acetylglutamate

107
Q

too much protein = what

A

buildup of nitrogen in body

108
Q

essentail amino acids are what

A

amino acids that cannot be synthesized by humans and must be obtained in the diet

109
Q

albinism defective enzyme

A

tyrosine 3-monooxygenase (tyrosinase)

110
Q

carbamoyl phosphate synthetase 1 deficiency defective enzyme

A

carbamoyl phosphate synthetase 1

111
Q

maple syrup urine disease other name

A

branched chain ketoaciduria

112
Q

maple syrup urine disease enzyme

A

branched chain alpha keto acid dehydrogenase complex

113
Q

phenylkeoturia defective enzyme

A

phenylalanine hydroxylase

114
Q

tyrosin 3-monooxygenase medical conditon

A

albinism

115
Q

carbamoyl phosphate synthetase 1 medical condition

A

carbamoyl phosphate synthetase 1 deficiency

116
Q

branched chain alpha keto acid dehydrogenase complex medical condition

A

maple syrup urine disease

117
Q

phenylalanine hydroxylase medical condition

A

phenylketonuria

118
Q

if issue with urea cycle enzymes, can treat with what

A

benzoate and/or phenylbutyrate

119
Q

valine, leucine, isoleucine go to alpha keto acids

A

male syrup urine disease

120
Q

3 amino acids involved in maple syrup urine disease

A

leucine, isoleucine, valine

121
Q

what is inhibited in maple syrup urine disease

A

branch chain alpha keto acid dehydrogenase complex

122
Q

what can maple syrup urine disease cause

A

mental degradation

123
Q

in phenylketonuria, what can’t be made

A

tyrosine

124
Q

what enzyme does PKU block

A

phenylalanine hydroxylase

125
Q

what does phenylalanine hydroxylase normally do

A

phenylalanine to tyrosine

126
Q

PKU results in what

A

accumulation of keto acids

127
Q

PKU makes what an essential amino acids

A

tyrosine, bc its production is blocked

128
Q

dipeptide absorbed and broken down to phenylalanine and something else

A

aspartane

129
Q

what can plants do that we can’t do (amino acids)

A

they can put N groups on C skeletons to form amino acids

130
Q

lightning and UV makes up what percent of Nitrogen cycle

A

15%

131
Q

industrial makes up what percent of nitrogen cycle

A

25%

132
Q

microorganisms make up what percent of nitrogen cycle

A

60%

133
Q

nitrogen fixation main enzyme

A

dinitrogenase

134
Q

most abundant gas in our atmosphere

A

molecular nitrogen

135
Q

electrons in nitrogen fixation

A

extensive e transfer

136
Q

how many ATP required per N2

A

16

137
Q

involves extensive transfer of e- eventually transferred

A

nitrogen fixation

138
Q

in amino acid synthesis, what is made first

A

carbon skeleton

139
Q

in amino acid synthesis, what happens second

A

transamination reaction to add amino group

140
Q

animals cannot synthesize what

A

EAA

141
Q

how many biosynthetic families are there

A

6

142
Q

when we synthesize AA, we use what as donors

A

glutamate and glutamine

143
Q

2 universal AA donors

A

glutamate and glutamine

144
Q

key in degradation and AA syn

A

transamination

145
Q

remove amino group from 1 AA to a keto acid, forms new AA

A

transamination

AGBI 410 (26 decks)

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