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Biochemistry > Chapter 21 AA metabolism > Flashcards

Chapter 21 AA metabolism Flashcards

(89 cards)

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1
Q

What are Essential AA

A

Arginine, Histidine, Isoleucine, Leucine, Lysine, Methionine, Phenylalanine, Threonine, Valine ( Ate Hotdogs In Lingerie, Lost My Pants Twerking Vigorously )

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2
Q

What the non-essential AA

A

Alanine, Asparagine, Aspartate, cysteine, Glutamate, Glutamine,
Glycine, Proline, Serine, Tyrosine ( Accidentally Aroused Academic Counselor, Got Ghosted, Gave Presentation Still Tipsy )

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3
Q

How are peptide bonds made into amino acids and does digestion happen in the mouth

A

Through hydrolysis and no digestion happen in the mouth

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4
Q

What acid denatures dietary protein in the stomach

A

HCl

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5
Q

_____ is activated by acid to make ________

A

Pepsinogen, pepsin

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6
Q

What does pepsin do and when is it stable and active

A

it hydrolyzes peptide bonds in denatured proteins making smaller polypeptide and it is stable and active at pH of 1-2

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7
Q

Where do the smaller polypeptide entire and why does the pepsin becomes inactive

A

they entire the small intestine where pepsin is inactive due to the less acidic environment

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8
Q

Pancreatic Zymogens are secreted and cleaved to activate what

A

Proteases (trypsin, chymotrypsin, and carboxypeptidase)

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9
Q

What is the purpose of proteases

A

to further hydrolyze the peptide bonds

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10
Q

Where do the free amino acids go

A

they are absorbed into the bloodstream

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11
Q

How are proteins mark for degradation

A

by covalently liking them to ubiquitin

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12
Q

what is AA pool and how do they enter

A

entire collection of AA in the body and enter through digestion or breakdown of old proteins

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13
Q

AA are used for the synthesis of ___ _______ biomolecules

A

new nitrogen

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14
Q

What are some places the AA pool contributes to

A

Tissue proteins, non-protein nitrogen compounds , transamination for urea excretion or amino groups for biosynthesis, and pyruvate, acetoacetate, acetyl-SCoA, TCA intermediate

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15
Q

What can pyruvate, acetoacetate, acetyl-SCoA, TCA intermediate from AA pool catabolic pathways turn in to

A

Fats via fatty acid biosynthesis, Ketone bodies via ketogenesis, Glucose via gluconeogenesis (which can all go to storage) and the TCA intermediates further go on to produce Energy

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16
Q

What is the general AA degradation scheme

A

Removal of amino group
use of N in synthesis of new nitrogen compounds
Passage of nitrogen into the urea cycle
Incorporation of the carbon atom into compounds that enter the TCA cycle

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17
Q

AA catabolism: Where do the parts of the AA go

A

NH3 goes to the urea cycle , and carbon skeleton can go into CO2 and H2O, Glucose, Acetyl-coA, and Ketone bodies

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18
Q

Can Humans store nitrogen, why or why not

A

No, N containing compounds and ammina is toxic to cells

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19
Q

Amino Nitrogen must be ___________ or___________

A

incorporated urea and excreted, or synthesis new compounds

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20
Q

what new compounds can amino nitrogen make

A

nitric oxide, Hormones, Neurotransmitters, Nicotinamide( NAD+/NADP+), Heme, or nucleic acids

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21
Q

what is a common intermediate that AA’s are metabolized through to loss ammonia

A

Glutamate ( AA-> Glutamate-> NH4+)

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22
Q

Transamination does what

A

the 1st removal of amino group to transfer to alpha-ketogluterate to make glutamate

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23
Q

what is amino transferase do

A

the amino group of AA and keto group of alpha-keto acid are interconverted

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24
Q

Most transaminase enzymes are specific for alpha-Ketoglutarate as the _______ ______

A

amino acceptor (work with many AA’s )

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25
The Glutamate made by transamination can be used to what
provide amino groups for synthesis of new amino acids ( most made this way are recycled to regenerate alpha- ketogutarate for more rxn)
26
Enzymes that catalyze transamination need what
coenzyme pyridoxal-5-phosphate (PLP)
27
What is PLP a derivative of
Vitamin B6
28
transamination Rxn are ______ reversible and when
easily , depending on concentrations
29
What are the most toxic to least toxic Nitrogen product
Ammonia, Urea, Ureic acid
30
Where is Urea made and where does it go
in the liver, then secreted into the blood stream and sequestered by kidneys for excretion.
31
Where do urea 2 nitrogen's come from and where do the carbons comes from
Ammonia and aspartate, HCO-3
32
What is the major reg. point in the urea cycle
Carbamoyl phosphate synthase 1
33
Carbamoyl phosphate is activated by what and when is it made
N-Acetyglutamate, which is made when glutamate and Acetly-CoA levels are high
34
What biomolecule comes from the Urea cycle to eventually form malate then to go into the OAA or TCA cycle
Fumarate
35
In the urea cycle what is the carbon atom removed as
CO2
36
What are the nitrogen atoms removed as in the urea cycle
NH4+ and urea
37
How many high energy phosphate bonds are broken in the Urea cycle
4
38
What AA breakdown to make pyruvate
Alanine, Cysteine, Glycine, serine, Threonine, Tryptophan (Almost Cried Getting Suspended Three Times )
39
What AA break down to make Succinyl-CoA
Isoleucine, Methionine, Threonine, Valine ( Injected Mitochondria to Vine)
40
What AA breakdown to make Acetyl-CoA
Isoleucine, Leucine, Lysine, Threonine (Inside Lecture Losing Time )
41
What AA breakdown to make Oxaloacetate
Asparagine, Aspartate
42
What AA breakdown to make Fumarate
Aspartate, Tyrosine, Phenylalanine ( ATP)
43
What AA breakdown to make alpha ketoglutarate
Arginine, Glutamate, Glutamine, Histidine, Proline ( Ass Grabs Got Her Probation)
44
What AA breakdown to make Acetoacetate
Leucine, Lysine, Phenylalanine, Tryptophan, Tyrosine (Licked Lab Pipette, Tasted Terrible )
45
What are ketogenic amino acids able to do
breakdown into ketone bodies, which serve as an alternative energy source during fasting or low-carb states. and they cannot be converted into glucose
46
What are glucogenic AA able to do
Glucogenic amino acids can be converted into glucose through gluconeogenesis. This helps maintain blood sugar levels and supplies energy to glucose-dependent tissues like the brain and red blood cells
47
What AA are both Ketogenic and glucogenic
Isoleucine Lysine Phenylalanine, tryptophan, tyrosine (I Love pickeled turkey toes )
48
Methionines are precursor of what molecule and what do they do
precursor to SAM and they are potent methylator agents
49
______ is generated from NADPH
THF
50
Which AA need energy imput to be degraded
Met, Trp, and Phe
51
What is the important coenzyme in amino acid metabolism that is derived from B6?
Pyridoxal phosphate (PLP) ## Footnote PLP is crucial for transamination, deamination, decarboxylation, and racemization
52
What is the key role of Pyridoxal phosphate (PLP) in metabolism?
Transfers amino groups between amino acids and α-keto acids ## Footnote PLP is derived from B6 (Pyridoxine)
53
Which coenzyme is associated with B9 and involved in one-carbon transfer reactions?
Tetrahydrofolate (THF) ## Footnote THF transfers methyl, methylene, and formyl groups during amino acid and nucleotide synthesis
54
What is the key role of Tetrahydrofolate (THF) in metabolism?
Transfers methyl, methylene, and formyl groups during amino acid and nucleotide synthesis ## Footnote THF is derived from B9 (Folate)
55
What is the important coenzyme in amino acid metabolism that is derived from B12?
Cobalamin (Vitamin B12) ## Footnote Cobalamin is involved in methyl group transfer and rearrangements
56
What is the key role of Cobalamin (Vitamin B12) in metabolism?
Works with THF; used in methionine synthesis and conversion of methylmalonyl-CoA to succinyl-CoA ## Footnote Cobalamin is derived from B12
57
Which coenzyme is associated with B7 and is involved in carboxylation?
Biotin ## Footnote Biotin adds CO₂ to substrates, such as converting propionyl-CoA to methylmalonyl-CoA
58
What is the key role of Biotin in metabolism?
Adds CO₂ to substrates ## Footnote Biotin is derived from B7
59
What are the coenzymes involved in redox reactions derived from B3?
NAD⁺ / NADP⁺ ## Footnote NAD⁺ / NADP⁺ are used in oxidative deamination and other oxidation steps
60
What is the key role of NAD⁺ / NADP⁺ in metabolism?
Used in oxidative deamination and other oxidation steps ## Footnote NAD⁺ / NADP⁺ are derived from B3 (Niacin)
61
Which coenzyme is associated with B2 and is often used in amino acid catabolism?
FAD ## Footnote FAD is involved in redox reactions, particularly in oxidative deamination
62
What is the key role of FAD in metabolism?
Often used in amino acid catabolism ## Footnote FAD is derived from B2 (Riboflavin)
63
______ Synthase is a control point which is vital for regulating nitrogen metabolism
Glutamine
64
glutamine synthetases are activated by what
Alpha-Ketoglutarate
65
Sulfur containing AA are made from homocysteine produced from _____________
S-adenosyl-homocysteine
66
67
What is Phenylketonuria (PKU)?
Phenylketonuria (PKU) is a genetic disorder in which the body cannot break down phenylalanine, an amino acid found in food. This leads to its accumulation, causing brain damage if untreated. ## Footnote PKU is an autosomal recessive disorder.
68
What enzyme is deficient in PKU, and what is its role in amino acid metabolism?
The enzyme phenylalanine hydroxylase (PAH) is deficient in PKU. PAH normally converts phenylalanine to tyrosine. Without PAH, phenylalanine accumulates, and tyrosine becomes an essential amino acid in affected individuals. ## Footnote Tyrosine is crucial for the synthesis of neurotransmitters.
69
What are the symptoms of untreated PKU?
Untreated PKU can lead to: * Intellectual disabilities * Seizures * Behavioral problems * Skin rashes * Microcephaly (small head size) * Musty odor due to phenylalanine build-up in urine ## Footnote Symptoms typically manifest within the first few months of life.
70
How is PKU diagnosed?
PKU is typically diagnosed through a newborn screening test that measures blood phenylalanine levels. Early detection is critical to prevent brain damage. ## Footnote Screening is usually done within the first week of life.
71
What is the treatment for PKU?
The main treatment for PKU is a phenylalanine-restricted diet (avoiding high-phenylalanine foods like meat, eggs, and dairy) combined with tyrosine supplementation. In some cases, sapropterin dihydrochloride (a PAH cofactor) can help increase PAH activity. ## Footnote Regular monitoring of blood phenylalanine levels is essential to manage the diet.
72
Fill in the blank: The enzyme _______ is deficient in PKU.
phenylalanine hydroxylase ## Footnote This deficiency leads to the accumulation of phenylalanine in the body.
73
True or False: PKU is an autosomal dominant disorder.
False ## Footnote PKU is an autosomal recessive disorder, requiring two copies of the mutated gene for the disorder to manifest.
74
where does Heme synthesis take place
Partly in mito and partly in cyto
75
what are the major sites of heme biosynthesis
erythroid cell and liver ( heme synthesis in erythroid cell is a one-time thing)
76
Porphyria's happen because
Heme biosynthesis has mutation or mis regulation
77
In the liver the level of heme synthesis depend on what
metabolic conditions
78
Heme is a source of ____ Prigments
Bile
79
what is heme degrade to in dying erythrocytes
bilirubin
80
jaundice is a build up of and what happens
bilirubin and cause a yellow color due to impaired liver, blocked bile
81
What hormones are derived from tyrosine
epinephrine, norepinephrine, dopamine
82
What hormones are derived from Tryptoph
Serotonin
83
What hormones are derived from Histidine
Histamine
84
What hormone is derived from Arginine and what does it do
Nitric oxide and it is a Vaso dilator
85
What strains of Bacteria can convert N2 to metabolically useful forms
Diazotrophs ( or bacteria that colonize the root nodules of legumes
86
Nitrogen complex are rare and O2 sensitive and requires at least ____ to do job of N2--> NH3
16 ATPS
87
N2 is _______ to lots of power , and is needed to do fixation
stable
88
Bacteria fix N2 to make what upon death
NH3 and AA
89
What two enzymes assimilates fixed nitrogen atoms into alpha-ketoglutarate to make glutamate, which can go on to make other AA through transamination
Glutamine synthase and Glutamate synthase

Biochemistry (3 decks)

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