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Medical Biochemistry > Degradation of Amino Acids > Flashcards

Degradation of Amino Acids Flashcards

Protein Digestion, Amino Acids, Tissue Utilization, Degradation of Amino Acids, Fate of Carbon Core, Urea Cycle

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USMLE® Step 1 flashcards
1
Q

BUN in pregnancy

A

decreased

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2
Q

other sources of alanine besides the muscle

A

kidney and intestines

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3
Q

CPSI deficiency

A

Type I hyperammonemia

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4
Q

the second step of urea cycle

A

citrulline synthesis

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5
Q

Aspartate + citrulline +ATP —> argininosuccinateWhat happes to the nitrogen of aspartate?

A

gets incorporated into urea

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6
Q

an alternative to low protein diet aimed at reducing the ammonia load on the urea cycle

A

scavenger drugs

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7
Q

BUN in liver damage

A

decreased

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8
Q

high levels of N-acetyl glutamate leads to

A

increased CPSI activity

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9
Q

blood citrulline level in type I and type II

A

low for both

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10
Q

Glutamate directly provides nitrogen (NH4+) to urea cycle through

A

deamination by glutamate dehydrogenase

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11
Q

The only place that urea cycle takes place in

A

liver

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12
Q

The two precursors of argininosuccinate

A

citrulline and aspartate

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13
Q

the reaction catalyzed by carbamoyl phosphate synthetase I

A

CO2 + NH4+ – 2ATP —> carbamoyl phosphate

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14
Q

Glutaminase

A

the enzyme in the kidney that forms NH4+ and glutamate from glutamine

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15
Q

ALT

A

alanine aminotransferase(Alanine/ a-ketoglutrate) and (pyruvate/ glutamate)

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16
Q

the amino acids that can undergo deamination

A

glutamate, glycine, serine, threonine, histidine

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17
Q

the product of the step of urea cycle is transported into the cytosol

A

second step. citrulline gets transported to cytosol

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18
Q

two methods for carbamoyl phosphate synthesis

A

1- Mitochondria- urea cycle and CPSI2- from glutamine and CO2 by CPSII in cytosol (–> pyrimidine synthesis)

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19
Q

when to provide arginine as urea cycle intermediate

A

if argininosuccinate lyase is defecient.

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20
Q

ALT level 36hours after ingestion of toxic mushroom

A

ALT reaches 20X its normal level after 36 hours.Indicates liver cell necrosis- liver as the site for toxic removal

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21
Q

the deficiency of argininosuccinate lyase cased

A

argininosuccinyl acidemia

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22
Q

the first step in urea synthesis

A

CO2 + NH4+ – 2ATP —> carbamoyl phosphate

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23
Q

function of glutamate dehydrogenase in other tissues , EXCEPT the liver and kidney

A

formation of glutamate and water from a-ketoglutarate and NADP+

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24
Q

argininemia is caused by

A

the deficiency of arginase which catalyzes the cleavage of arginine

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25
Q

main detoxification reaction in brain is catalyzed by this enzymeHint: 1/3 enzymes that fixes free ammonia

A

glutamine synthetase

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26
Q

the coenzyme of transaminase

A

PLP- pyridoxal phosphate

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27
Q

deamidation

A

removal of amide group from glutamine and asparagine as NH4+

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28
Q

BUN and blood ammonia in liver damage

A

BUN decreased in liver damage But blood ammonia increased during liver damage

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29
Q

importance and the enzyme deamidation of glutamine in kidney

A

important in kidneyprovides most of the NH4+ in the urineNH3 aids the secretion of protons into the urine and indirectly helps to balance blood PH.Glutaminase is the enzyme

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30
Q

the fate of fumarate as a by product of arginine synthesis (argininosuccinate lyase)

A

enters the TCA cycle and regenerate oxaloacetate and then aspartate.

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31
Q

carbamoyl phosphate synthesis of urea cycle takes place in

A

mitochondria

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32
Q

blood nitrogen metabolites

A

blood urea nitrogen (BUN)creatinine uric acidammonia

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33
Q

The impact of high levels of arginine production on urea production

A

increased urea production though1- high n-acetyl glutamate –> increased CPSI –> increased urea production2- increased ornithine production –> increased urea production

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34
Q

BUN in kidney damage

A

increased

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35
Q

how to reduce ammonia load on the urea cycle

A

low protein diet, avoid fasting - to limit amino acid degradation

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36
Q

Nitrogen is carried to the liver by

A

alanine and glutamine

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37
Q

activates CPSI

A

N-acetyl glutamate

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38
Q

The two amino acids that undergo deamidation

A

glutamine and asparagine

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39
Q

name at least three condition in which plasma ALT And AST are elevated

A

cirrhosishepatitisliver toxicity

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40
Q

Glutamine —?—> glutamate —?–> a-KGLIVER

A

GlutaminaseGDH

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41
Q

cleavage of arginine into urea and ornithine is catalyzed by

A

arginase

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42
Q

the only way arginie is produced in human body

A

arginine synthesis via argininosuccinate lyase in cytosolArgininosucccinate —> fumarate + arginine

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43
Q

arginase cleaves argininie into

A

urea and ornithine

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44
Q

conversion of glutamine to alanine

A

glutamine first to glutamate- E: glutaminaseGlutamate to alanine- E- ALLT

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45
Q

the central role of glutamate in nitrogen removal

A

transamination - collect nitrogendeamination- provides nitrogen to the urea cycle by glutamate dehydrogenasetransaminating oxaloacetate into asparte- provides nitrogen indirectly to the urea cycle. Aspartate then provides an amino group to ureaprecursor for the allosteric activator of the urea cycle

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46
Q

high levels of arginine leads to

A

high levels of N-acetyl-glutamateIncreased ornithine production

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47
Q

the energy requirement of argininosuccinate synthesis

A

1 ATP

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48
Q

the energetics of the urea cycle

A

aspartate + NH3 + CO2 +3ATP –> Urea + fumarate + 2ATP + 2P + PP + 3H2o

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49
Q

Increased CPSI activity leads to

A

Increased urea production

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50
Q

energy requirement of carbamoyl phosphate synthesis for urea cycle

A

2ATP

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51
Q

Increased ornithine production leads to

A

increased urea production

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52
Q

The allosteric regulator of CPSI

A

N-acetyl-glutamate

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53
Q

how to limit amino acid degradation

A

low protein diet and avoid fasting

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54
Q

CPSI or N-acetylglutamate synthase deficiency causes

A

Type I hyperammonemia

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55
Q

the only X-linked recessive primary hyperammonemias

A

type II hyperamoonemia- ornithine transcarbamoylase

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56
Q

argininosuccinate synthesis takes place in

A

cytosol

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57
Q

after citrulline synthesis, it is transported to the

A

cytosol

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58
Q

Urine orotate for type I a nd type II

A

type I - lowType II- HighThe only differentiating factors. Other values are identical for the two.

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59
Q

ornithine transcarbamoylase catalyzes the synthesis of ——– in ——.

A

citrulline in mitochondria

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60
Q

amino acid degradation takes place in all tissues. How does nitrogen gets to the liver?

A

Nitrogen is carried to the liver by ALANINCE and GLUTAMINE

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61
Q

defeciency in ornithine transcarbamoylase

A

type II hyperammonemia

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62
Q

aminotransferase

A

transaminase- an enzyme for the reversible reaction of transamination.

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63
Q

activates the synthesis of N-Acetylglutamate

A

HIGH levels of arginine

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64
Q

as the utilization of amino acids decreases, urea production ——

A

decreases

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65
Q

deamination

A

removal of a-amino group from certain amino acids as NH4+glutamate, glycine, serine, threonine, histidine

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66
Q

net glutamine producers

A

muscle and brain

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67
Q

PLP

A

pyridoxal phosphate

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68
Q

The role of glutamate in the following reactionGlutamate + Acetyl-CoA –> N-acetyl Glutamate

A

1- allosteric activator2- provides nitrogen

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69
Q

blood ammonia in urea cycle disorders

A

increased

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70
Q

how many high energy phosphate bonds are broken and what does it mean for the urea cycle

A

4 high energy bonds are broken, which makes the cycle irreversible

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71
Q

how can part of the used energy in urea cycle be recovered?

A

if fumarate enters the TCA cycleFumarate –> Malate _> Oxaloacertate–> Aspartate and 1 NADH ~ 2.5 ATP through oxidative phosphorylation

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72
Q

CPSI

A

carbomyl phosphate synthetase I catalyzes the carbamoyl phosphate synthesis- The rate limiting and committed step of urea cycle

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73
Q

three enzymes that can fix free ammonia into organic molecules

A

glutamate dehydrogenaseglutamine synthetasecarbamoyl phosphate synthetaseI

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74
Q

The reason for decreased level of nitrogen metabolites during pregnancy

A

increased GFR

75
Q

Glutamine –?–> glutamate —?–> alanine

A

glutaminase, ALT

76
Q

The main pathway of amino acid nitrogen removal is

A

transamination

77
Q

Citrulliunuria type I

A

deficiency of argininosuccinate synthase

78
Q

the benefit of limiting amino acid degradation

A

reducing the ammonia load in the urea cycle

79
Q

the autosomal recessive primary hyperammonemias

A

type I, citrullinuria type I, argininosuccinic acidemiaargininemia

80
Q

arginine synthesis is catalyzed by

A

argininosuccinate lyase

81
Q

the rate limiting and committing step of the urea cycle is

A

carbamoyl phosphate synthesis

82
Q

transamination

A

transfer of an a-amino group from an amino acid to an a-keto acid

83
Q

is a precursor for the allosteric activator of the urea cycle

A

glutamate

84
Q

the role of citrulline suppliment in type I and II hyperammonemia

A

to capture aspartate so at least one nitrogen can be excreted

85
Q

deficiency causes citrullinuria type I

A

argininosuccinate synthetase

86
Q

1—- + 2—- –(GDH)—> NADP+ + Glutamatemuscle and peripheral tissues

A

a-KG + NH4+required for glutamine transport

87
Q

during transamination, the amino acid nitrogen is generally collected on

A

glutamate

88
Q

main glutamine users

A

kidney, gut, immune cells and liver

89
Q

Three ways to supply the amino acid pool

A

1- degradation of bodies own protein (endogenous)2- degradation of dietary protein (exogenous)3- synth. of non-essential aa from other pathways

90
Q

glutamate indirectly provides nitrogen to urea by

A

transaminating oxaloacetate into aspartate. Aspartate then provides an amino group to urea.

91
Q

high levels of ALT and AST in plasma indicates

A

liver damage

92
Q

the reaction catalyzed by glutamate dehydrogenase

A

a-ketoglu + NH4+ glutamate

93
Q

blood arginine level for type I and type II

A

both low

94
Q

blood NH3 level for type I and type II

A

both high

95
Q

starvation and the brain

A

during starvation the brain switches from glucose to ketone bodies (MAINLY FROM FATTY ACIDS) as energy source.

96
Q

glutamate dehydrogenaseresults in the formation of these compound in the kidney and liver

A

NADPH, a-ketoflutarate, NH4+ and H+Substrate: Glutamate and HOH

97
Q

Urea is transported to the —— and excreted in ——–. some urea leaves through the —–, too.

A

urea transported to the kidney and excreted in urine.some urea leaves through intestine

98
Q

the transamination reaction is —— and ——- catalyzes the reaction.

A

reversible, transaminase (aminotransferase)

99
Q

citrulline and aspartate form argininosuccinate. what is the source of aspartate?

A

aspartate is produced by transamination of oxaloacetate (AST) and the aspartate nitrogen will incorporate into urea

100
Q

fasting and muscle proteins

A

during fasting muscle proteins are degraded and amino acids are transported to the liver and converted to glucose.And the Nitrogen of the used amino are converted to urea.

101
Q

scavenger drug for glycine

A

benzoate + glycine –> hippuric acid –> excretion

102
Q

pyridoxine

A

B6

103
Q

treatment of urea cycle disorders

A

a- reduce the ammonia load on the urea cycleb- provide urea cycle intermediates

104
Q

cleavage of arginine into urea and ornithine takes place in

A

the cytosol

105
Q

the first step in urea synthesis is catalyzed by

A

carbamoyl phosphate synthetase I

106
Q

blood ammonia in liver damage

A

increased

107
Q

NAME?

A

N-acetylglutamate

108
Q

amino acid degradation takes place in

A

all tissues

109
Q

deficiency of arginase causes

A

argininemia

110
Q

argininosuccinate synthesis is catalyzed by

A

argininosuccinate synthetase

111
Q

arginine as a reactant for nitric oxide synthesis

A

Arginine +NADPH + O2 –> citrulline +NO + NADP+ + H2O

112
Q

it can provide nitrogen both directly and indirectly to the urea cycle

A

glutamate

113
Q

citrulline synthesis is catalyzed by

A

ornithine transcarbamoylase

114
Q

the precursors of N-acetyl glutamate

A

glutamate and Acetyl CoA

115
Q

The role of Arginine in the following reaction:Glutamate + Acetyl-CoA –> N-acetyl Glutamate

A

Arginine is + (activator)

116
Q

ALT specificity vs AST

A

ALT is more specific

117
Q

CPSII

A

the enzyme for carbanmoyl phosphate synthesis in the cytosol from glutamine and CO2

118
Q

BUN and blood creatinine in kidney damage

A

increased

119
Q

the first two intermediates of the urea cycles which are made in the mitochondria

A

carbamoyl phosphate and citrulline

120
Q

urea cycle starts in —– and is completed in the —–.

A

starts in mitochondria and completed in cytosol.

121
Q

the major reaction in the muscles that constitute the main source of alanine

A

protein degradation and transamination

122
Q

AST

A

aspartate aminotransferase(Oxaloacetate/glutamate) and (Aspartate/a-ketoglutrate)

123
Q

scavenger drug for glutamine

A

Phenylbutyrate

124
Q

BUN, blood creatinine and blood uric acid level during pregnancy

A

decreased

125
Q

its deficiency causes argininosuccynyl acidemia

A

argininosuccinate lyase

126
Q

sources of alanine- alanine transport to the liver: Glucose/Alanine Cycle

A

main: muscle (result of protein degradation and transamination)Other: kidney and intestine (conversion of glutamine to alanine)

127
Q

Blood creatinine in kidney damage

A

increased

128
Q

scavenger drugs

A

conjugate amino acids and target them for urinary excretion

129
Q

this vitamin is required for PLP formation

A

Vitamin B6- pyridoxine

130
Q

The third step of urea cycle

A

argininoscuccinate synthesis

131
Q

transports ornithine into the mitochondria from the cytosol

A

ornithine translocase

132
Q

ornithine translocase

A

transports ornithine into the mitochondria from the cytosol

133
Q

blood uric acid in pregnancy

A

decreased

134
Q

conditions that resemble fasting as well as high protein diet and excessive degradation ——– urea synthesis and —— synthesis of urea cycle enzymes.

A

increase, increase

135
Q

arginine —> urea and ornithineE: arginasethe fate of the arginine and ornithine

A

arginine cab be used by other pathways: protein synthesis and nitric oxide synthesisornithine moves back to mitochondria and reacts with another molecule of carbamoyl phosphate

136
Q

the reactions that lead to the formation of alanine in kidney and intestine

A

conversion of glutamine to alanine

137
Q

the reaction catalyzed by glutamine synthetase

A

Glutamate + NH4+ —– ATP —> glutamine

138
Q

the product of transamination of oxaloacetate (AST)

A

aspartate

139
Q

arginine synthesis takes place in

A

cytosol

140
Q

blood uric acid in gout

A

increased

141
Q

diagnostic tool for primary hyperammonemias

A

metabolites before the deficiency accumulates in blood/ urine.Metabolites after the deficiency have much lower levels.

142
Q

The central role of glutamate in nitrogen removal- 3 general descriptions

A

precursor for allosteric activatorProvides nitrogen in two different wayscollects nitrogen

143
Q

when to provide citrulline supplement as urea cycle intermediate

A

In type I and II hyperammonemia.it captures aspartate, so at least one nitrogen can be excreted

144
Q

Three general ways to deplete amino acid pool

A

1- protein synthesis for the body2- consumption of aa as precursor for small nitrogen containing molecules3- conversion of amino acids to glucose, glycogen, a-Kbodies, and fatty acid oroxidation to Co2 and H2o

145
Q

regulation of the urea cycle

A

N-acetylglutamate (allosteric activator)High arginine levelHigh protein diet and excessive degradationand the concentration of substrate and intermediates

146
Q

Blood creatinine in pregnancy

A

decreased

147
Q

arginine supplement for argininosuccinate lyase deficiency

A

it generates more ornithine for urea cycle to continue.also, catalyzes the production of N-acetylglutamate so acceelerates CPSI

148
Q

The two main purposes for the transport of alanine to the liver

A

1- removal of nitrogen through the urea cycle2- glucogeogenesis

149
Q

1—- + 2—– -(glutamine synthetase)–> glutamine + ADP Muscle and peripheral tissue

A

glutamineRequired fro glutamine transport

150
Q

objFate of carbon core of amino acid depends on the nutritional state of the body.Fate of Carbon core of aa in the fed state:

A

Energy storageThe carbon of the excess amino acids will be converted to:1- glucose –> Glycogen2-acetylCoa –> TAG

151
Q

objFate of carbon core of amino acid depends on the nutritional state of the body.Fate of Carbon core of aa in the fasting state

A

Energy productionCo2pyruvateTCA int.Acetyl CoA- Acetoacetate

152
Q

What is common to both the fed and fasting states with respect to the fate of the carbon core of aa:

A

In both, amino acids are constantly used for the synthesis of physiologically important metabolites - proteins and hormones

153
Q

obj ketogenic amino acids

A

leucine, lysine

154
Q

objglucogenic aa

A

non essentialsAlaArgAsnAspCysGluGlnGlyPro Seress. aa.HisMetThrVal

155
Q

Objnoess. aa.

A

AlaArgAsnAspCysGluGlnGlyPro SerTyrosine ( glucogenic and ketogenic)The rest are glucogenic

156
Q

objthe glucogenic noess. aa.

A

AlaArgAsnAspCysGluGlnGlyPro Ser

157
Q

objthe glucogenic and ketogenic noess aa.

A

tyr

158
Q

objthe glucogenic and ketogenic ess.aa.

A

ThrIsoPheTrp

159
Q

objconditionally ess. aa.

A

tyr, Arg, Cys

160
Q

objThe surplus of cystine (cond. ess. aa.) comes from

A

met (ess, glucogenic)

161
Q

objTyr (cond. ess. aa./ glucogenic and ketogenic) is produced from

A

phenyl-alanince (gluco-ketogenic)

162
Q

objConditionally essential Arg

A

Arg is not ess. for adults, byt it is ess. for children

163
Q

the aa that is ess for only children

A

Arg

164
Q

Tyr production

A

Tyr is produced by the hydroxylation of phenyl-alanine

165
Q

the source for carbon cores of 10-essentional aa.

A

glucose

166
Q

ObjThe 10 ess. aa

A

Glucogenic: His, Met, Thr, Val.Gluco/Keto: Thr, ILe, Phe, TrpKet: leu, Lys

167
Q

All the ketogenic aa. are

A

essentionalLeu, Lys

168
Q

aa. syn. f. glycolysis int.

A

Cys, Gly, Ser, Ala

169
Q

aa syn. f. OxA

A

Asp, Asn

170
Q

aa. syn. f. a-ketoglutrate

A

Glu, Gln, Pro, Arg

171
Q

The lonely aa.(an amino acid that is not produced via any three common pathways: f. OxA, F. a-ketoglutrjate and f. gly int.)

A

tyrosine, which is produced by the hydroxylation of phenylalanine.

172
Q

Coenz. fo. transamination (TA) and deamination (DA)

A

pyridoxal-phosphate (B6)

173
Q

B6

A

pyridoxal phosphate- a conenzyme for deamination and transamination

174
Q

Coenz. fo. metabolism of Ser, Gly, Met, His

A

Tetrahydrofolate (folate)

175
Q

Tetrahydrofolate

A

coenzyme fo. metabolism of gly, his, met, ser

176
Q

cobalamins

A

B12 (Met metabolism conezyme)

177
Q

B12 as a conenzyme

A

B12- Cobalamins is a conezyme for methionine metabolism

178
Q

BH4

A

tetra-hydro.biopterin

179
Q

tetrahydrobipterin is synthesized from

A

GTP

180
Q

Tetrahydrobiopterine (BH4) is a conezyme for

A

hydroxylation of phenylalanine, tyr and trp

181
Q

Hydroxylation of Phe, Tyr, Trp iis assisted by this coenzyme

A

BH4- tetrahydrobioptrein

182
Q

The coenzyme for oxidative decarboxylation of BCAA

A

Thiamine-Pyrophosphate (B1) and lipoate

183
Q

Thiamine-pyrophosphate and lipoate are common coenzymes for

A

oxidative decarboxylation of BCAA.thiamine-pyrophosphate is B1

184
Q

Other names for B1, B6 and B12

A

B1- thiaminepyrophosphateB6- pyridoxal phosphateB12 cobalamins

Medical Biochemistry (12 decks)

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