Harper's Biochemistry Chapter 27 - Biosynthesis of the Nutritionally Nonessential Amino Acids

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Questions and Answers

Which amino acid is primarily synthesized from homocysteine and is not considered nutritionally essential?

  • L-Serine
  • L-Tyrosine
  • L-Cysteine (correct)
  • L-Proline

What is the main precursor for the synthesis of glycine in mammals?

  • Serine (correct)
  • Choline
  • Alanine
  • Glutamate

Why is dietary tyrosine not able to replace phenylalanine in the diet?

  • Phenylalanine is nonessential and can be synthesized from other amino acids.
  • Tyrosine has no dietary significance.
  • The conversion of phenylalanine to tyrosine is irreversible. (correct)
  • Tyrosine can be converted to phenylalanine.

Which pathway accurately describes the initial step in proline biosynthesis?

<p>Glutamate's γ-carboxy group is converted to an anhydride. (A)</p> Signup and view all the answers

Which reaction results in the formation of alanine through transamination?

<p>Pyruvate to Alanine (C)</p> Signup and view all the answers

What additional routes exist for glycine formation in mammals?

<p>From serine and choline (D)</p> Signup and view all the answers

In collagen biosynthesis, hydroxyproline and hydroxylysine are important. What is a key characteristic of these amino acids?

<p>They are formed post-translationally. (C)</p> Signup and view all the answers

Which enzyme catalyzes the synthesis of asparagine from aspartate?

<p>Asparagine synthetase (A)</p> Signup and view all the answers

What role does tetrahydrobiopterin play in the metabolism of phenylalanine?

<p>It provides reducing power derived from NADPH. (D)</p> Signup and view all the answers

Which metabolic pathway is involved in producing glycine aside from transamination?

<p>Serine biosynthesis (B)</p> Signup and view all the answers

The reaction dependent on Mg-ATP is characteristic of which amino acid synthesizing enzyme?

<p>Asparagine synthetase (A)</p> Signup and view all the answers

Which of these amino acids is considered a nonessential amino acid due to its synthesis in the body?

<p>Aspartate (A)</p> Signup and view all the answers

What is a significant feature of the transamination reaction between pyruvate and glutamate?

<p>It results in alpha-ketoglutarate. (C)</p> Signup and view all the answers

What is the primary role of asparagine in amino acid metabolism?

<p>To serve as a precursor for glutamate synthesis (C)</p> Signup and view all the answers

What is the intermediate formed during the conversion of glutamate to glutamine?

<p>γ-glutamyl phosphate (A)</p> Signup and view all the answers

Which enzyme is responsible for the conversion of 3-phosphoglycerate to serine?

<p>3-phosphoglycerate dehydrogenase (C)</p> Signup and view all the answers

Which amino acid conversion process is characterized by the use of both ammonium ion and glutamine as nitrogen sources?

<p>Aspartate to asparagine (C)</p> Signup and view all the answers

What is the consequence of the coupled hydrolysis of PPi to Pi in the asparagine synthesis reaction?

<p>It strongly favors the synthesis of asparagine (C)</p> Signup and view all the answers

Which compound provides the nitrogen in the enzyme-catalyzed reaction converting aspartate to asparagine?

<p>Glutamine (C)</p> Signup and view all the answers

Which factor directly influences the cytotoxic ammonium ion concentration during the synthesis of glutamate?

<p>The reductive amidation of α-ketoglutarate (A)</p> Signup and view all the answers

What type of reaction is the conversion of glutamate to glutamine primarily categorized as?

<p>Amidation (A)</p> Signup and view all the answers

In what metabolic pathway is the 3-phosphoglycerate dehydrogenase involved?

<p>Glycolysis (A)</p> Signup and view all the answers

What is the fate of the γ-amino group of the tetrahedral intermediate during the glutamine synthesis process?

<p>It is released as a proton (D)</p> Signup and view all the answers

Which statement about the synthesis of tyrosine is true?

<p>Tyrosine is classified as nutritionally semiessential. (C)</p> Signup and view all the answers

What role do glutamate dehydrogenase and glutamine synthetase play in amino acid biosynthesis?

<p>They help incorporate the ammonium ion into amino acids. (A)</p> Signup and view all the answers

In individuals suffering from Marasmus, which amino acid synthesis deficiency could contribute to their condition?

<p>Inadequate synthesis of tyrosine. (A)</p> Signup and view all the answers

Which amino acid is derived from the posttranslational modifications seen in collagen biosynthesis?

<p>Proline (A)</p> Signup and view all the answers

What distinguishes nonessential amino acids from essential amino acids?

<p>Nonessential amino acids can be synthesized by the body, though not always efficiently. (A)</p> Signup and view all the answers

Which pathway is involved in the biosynthesis of amino acids that include potentially toxic ammonium ions?

<p>Combined enzymatic actions of multiple amino acid biosynthesis pathways. (A)</p> Signup and view all the answers

What is a significant consequence of Menkes Syndrome on amino acid metabolism?

<p>Impaired copper transport affecting collagen formation. (B)</p> Signup and view all the answers

Which amino acid is not derived from the amino acids typically classified as nutritionally semiessential?

<p>Cysteine (C)</p> Signup and view all the answers

Which statement is true regarding posttranslational modifications in amino acids?

<p>They may lead to the formation of unique structural features in proteins. (D)</p> Signup and view all the answers

In the context of amino acid synthesis, what is a key reason why young children might experience growth issues?

<p>Insufficient production of nutritionally semiessential amino acids. (B)</p> Signup and view all the answers

Which amino acids are classified as nutritionally essential according to their roles in tissue aminotransferase reactions?

<p>Valine, Leucine, Isoleucine (D)</p> Signup and view all the answers

What is the enzymatic activity associated with the conversion of phenylalanine to tyrosine?

<p>Hydroxylation that involves a co-factor deficiency (B)</p> Signup and view all the answers

Which of the following elements is NOT necessary for the hydroxylation of proline and lysine during collagen synthesis?

<p>Calcium (C)</p> Signup and view all the answers

In Menkes Syndrome, which bioelement is particularly deficient, impacting copper utilization?

<p>Copper (C)</p> Signup and view all the answers

Which term describes amino acids that must be obtained from the diet due to the body's inability to synthesize them?

<p>Nutritionally essential amino acids (B)</p> Signup and view all the answers

What is the outcome when there is a deficiency of vitamin C in collagen biosynthesis?

<p>Impaired stability of collagen and scurvy development (B)</p> Signup and view all the answers

Which amino acid is derived from the decarboxylation of α-ketoglutarate during metabolism?

<p>Proline (C)</p> Signup and view all the answers

In the context of metabolic pathways, what is the primary role of aminotransferases regarding essential amino acids?

<p>Interconverting amino acids and their corresponding α-keto acids (B)</p> Signup and view all the answers

Which of the following conditions is NOT associated with a deficiency in protein energy intake?

<p>Diabetes mellitus (D)</p> Signup and view all the answers

Which of the following vitamins is essential for the reduction of dihydrobiopterin during amino acid metabolism?

<p>Vitamin C (B)</p> Signup and view all the answers

What condition is characterized by a dietary deficiency of vitamin C leading to bleeding gums and poor wound healing?

<p>Scurvy (D)</p> Signup and view all the answers

Which disorder results from a lack of copper, affecting collagen biosynthesis and leading to symptoms like kinky hair and growth retardation?

<p>Menkes syndrome (C)</p> Signup and view all the answers

Which disorder is caused by an impaired ability of connective tissue to form peptidy 4-hydroxyproline and 5-hydroxylysine due to nutritional deficiencies?

<p>Ehlers-Danlos syndrome (D)</p> Signup and view all the answers

What condition might develop in a child weaned onto a starchy diet that lacks sufficient protein and calories?

<p>Kwashiorkor (B)</p> Signup and view all the answers

Which amino acid deficiencies can result in unstable collagen structure and lead to connective tissue disorders?

<p>Proline and hydroxyproline (C)</p> Signup and view all the answers

Which genetic disorder is characterized by fragile bones and a deficiency in collagen synthesis?

<p>Osteogenesis imperfecta (D)</p> Signup and view all the answers

What is a potential outcome of both caloric intake and specific amino acid deficiencies in patients with short bowel syndrome?

<p>Marasmus (B)</p> Signup and view all the answers

What is the condition that results from a child being weaned onto a starchy diet lacking in protein?

<p>Kwashiorkor (C)</p> Signup and view all the answers

Which amino acid requires the most enzymatic steps for its synthesis according to the provided data?

<p>Arginine (A)</p> Signup and view all the answers

What type of dietary deficiency is predominantly associated with both kwashiorkor and marasmus?

<p>Protein deficiency (A)</p> Signup and view all the answers

How many total enzymes are required for the synthesis of nutritionally nonessential amino acids as listed?

<p>17 (A)</p> Signup and view all the answers

Which of the following amino acids is NOT classified as nutritionally essential?

<p>Glycine (B)</p> Signup and view all the answers

In the context of amino acid metabolism, what is a significant characteristic of marasmus?

<p>Overall caloric deficiency (A)</p> Signup and view all the answers

Which nutritionally essential amino acid requires both shared and non-shared enzymatic steps for its synthesis?

<p>Isoleucine (A)</p> Signup and view all the answers

Which of the following disorders is linked to specific amino acid metabolism due to deficiency?

<p>Kwashiorkor (D)</p> Signup and view all the answers

What dietary component is specifically mentioned as poor sources leading to amino acid deficiency in certain regions?

<p>Grains (B)</p> Signup and view all the answers

Which specific elongation factor is involved in recognizing selenocysteyl-tRNASec for incorporation into proteins?

<p>Selenocysteine insertion sequence binding protein (C)</p> Signup and view all the answers

What role do both procollagen-proline 4-hydroxylase and procollagen-lysine 5-hydroxylase play in collagen biosynthesis?

<p>They catalyze mixed-function oxidase reactions that incorporate molecular oxygen. (B)</p> Signup and view all the answers

Which compound serves as a substrate for the production of cysteine in the body?

<p>Homocysteine (B)</p> Signup and view all the answers

Which enzyme is crucial for the redox reactions involving selenocysteine in the human body?

<p>Thioredoxin reductase (C)</p> Signup and view all the answers

What is the likely impact of a deficiency in vitamin C on collagen synthesis?

<p>It would lead to improper cross-linking of collagen fibers. (C)</p> Signup and view all the answers

What is the primary reaction that converts glutamate to proline in biosynthesis?

<p>Reduction following cyclization of glutamate γ-semialdehyde (A)</p> Signup and view all the answers

Which enzyme is responsible for the hydrolytic removal of the phosphoryl group from phosphoserine?

<p>Phosphoserine hydrolase (D)</p> Signup and view all the answers

What is a significant characteristic of the reaction converting phenylalanine to tyrosine?

<p>It requires tetrahydrobiopterin as a cofactor. (D)</p> Signup and view all the answers

What is the ultimate precursor for cysteine synthesis in terms of nutritional importance?

<p>Methionine (C)</p> Signup and view all the answers

Which of the following statements about hydroxylated amino acids is true?

<p>They do not have specific tRNAs for incorporation during translation. (C)</p> Signup and view all the answers

In the metabolic pathway of phenylalanine to tyrosine, what is the fate of the oxygen atoms involved in the reaction?

<p>Both atoms are reduced to form water. (A)</p> Signup and view all the answers

What distinguishes the transformation of 3-phosphoglycerate to serine in amino acid metabolism?

<p>It requires the action of a dehydrogenase enzyme. (A)</p> Signup and view all the answers

Which amino acid is derived from the hydrolysis of cystathionine?

<p>Cysteine (D)</p> Signup and view all the answers

In collagen biosynthesis, what role do hydroxyproline and hydroxylysine play?

<p>They enhance protein stability through cross-linking. (D)</p> Signup and view all the answers

What is the significance of the reaction catalyzed by cystathionine β-synthase in amino acid metabolism?

<p>It links homocysteine and serine to form cystathionine. (C)</p> Signup and view all the answers

What is the key product formed from the amidation of glutamate catalyzed by glutamine synthetase?

<p>Glutamine (D)</p> Signup and view all the answers

Which intermediate is formed during the conversion of glutamate to glutamine?

<p>γ-Glutamyl phosphate (C)</p> Signup and view all the answers

What role does the hydrolysis of PPi to Pi play in the synthesis of asparagine?

<p>It strongly favors the reaction. (C)</p> Signup and view all the answers

Which enzyme catalyzes the reaction that produces serine from 3-phosphoglycerate?

<p>3-Phosphoglycerate dehydrogenase (D)</p> Signup and view all the answers

Which amino acid synthesis utilizes both ammonium ion and glutamine as nitrogen sources?

<p>Asparagine (A)</p> Signup and view all the answers

During the synthesis of glutamate, what is the primary effect of reducing ammonium ion concentration?

<p>It promotes more glutamate synthesis. (C)</p> Signup and view all the answers

What is the function of NH4+ in bacterial asparagine synthetases?

<p>It provides a nitrogen source. (C)</p> Signup and view all the answers

Which reaction type does the conversion of aspartate to asparagine primarily represent?

<p>Amidation (B)</p> Signup and view all the answers

In terms of enzymatic activity, what initiates the reaction for the formation of γ-glutamyl phosphate during glutamine synthesis?

<p>Binding of glutamate (A)</p> Signup and view all the answers

What is the final product released after the dephosphorylation step in the formation of serine from 3-phosphoglycerate?

<p>Serine (A)</p> Signup and view all the answers

Match the following terms related to amino acids with their correct definitions:

<p>Essential amino acids = Must be obtained from the diet Nutritionally nonessential amino acids = Can be synthesized by the body Transaminases = Enzymes that facilitate amino acid metabolism Scurvy = Disorder caused by vitamin C deficiency</p> Signup and view all the answers

Match the following amino acids with their associated biosynthesis precursors:

<p>Aspartate = Oxaloacetate Glutamate = α-Ketoglutarate Serine = 3-Phosphoglycerate Glycine = Threonine</p> Signup and view all the answers

Match the vitamin with its role in amino acid metabolism:

<p>Vitamin C = Prevents scurvy by aiding collagen synthesis Folate = Involved in amino acid metabolism Vitamin B6 = Coenzyme in transamination reactions Vitamin E = Antioxidant that protects cellular membranes</p> Signup and view all the answers

Match the following amino acids with their nutritional classification:

<p>Phenylalanine = Essential Glycine = Nutritionally nonessential Valine = Essential Glutamine = Nutritionally nonessential</p> Signup and view all the answers

Match the following amino acids with their role in collagen biosynthesis:

<p>Hydroxyproline = Stabilizes collagen structure Hydroxylysine = Involved in cross-linking of collagen Proline = Precursor for hydroxyproline Lysine = Precursor for hydroxylysine</p> Signup and view all the answers

Match the following terms with their correct definitions:

<p>Nutritionally essential amino acids = Amino acids that must be present in the human diet Nutritionally nonessential amino acids = Amino acids that do not need to be present in the diet Biosynthesis = The process of producing complex molecules from simpler ones ATP = A molecule that provides energy for biological processes</p> Signup and view all the answers

Match the following classes of amino acids with their numbers:

<p>Essential amino acids = 8 Nonessential amino acids = 12 Total common amino acids = 20 Enzymes for essential amino acids synthesis = Large relative to nonessential</p> Signup and view all the answers

Match the following descriptions with the appropriate terms:

<p>Plants and bacteria = Organisms that can synthesize certain amino acids Humans = Organisms that must obtain certain amino acids through diet Metabolically essential amino acids = Amino acids important for metabolism Reactions in biosynthesis = Chemical processes that produce amino acids</p> Signup and view all the answers

Match the following historical aspects with their significance:

<p>1930s = Period when the distinction of essential and nonessential amino acids was established Purified amino acids diet = Used to investigate amino acid requirements Neglect of certain biosynthesis pathways = Not discussed for humans in the context of amino acid Survival advantage = Benefit for retaining the ability to biosynthesize certain amino acids</p> Signup and view all the answers

Match the following features to their correct descriptions:

<p>Nutritionally essential = Must be ingested from food Nutritionally nonessential = Can be synthesized in the body Chemical reactions = Processes determining amino acid formation Dietary implications = Impact on amino acid availability for health</p> Signup and view all the answers

Flashcards

Valine, Leucine, Isoleucine

Nutritionally essential amino acids interconverted by tissue aminotransferases.

Amino acid interconversion

Tissue aminotransferases reversibly convert amino acids and their corresponding α-keto acids.

Proline Biosynthesis

Involves glutamate-5-kinase, glutamate-5-semialdehyde dehydrogenase, pyrroline-5-carboxylate reductase.

Wound Healing (Vit. C)

Vitamin C is needed for collagen stability; deficiency causes scurvy.

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Proline/Lysine Hydroxylation

Requires molecular oxygen, ascorbate, Fe2+, and α-ketoglutarate; involves mixed-function oxidases.

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Phenylalanine to Tyrosine

Conversion catalysed by phenylalanine hydroxylase, involves two enzymatic activities.

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Scurvy

Vitamin C deficiency resulting weakened collagen, leading to poor wound healing.

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α-ketoglutarate

A crucial molecule involved in proline/lysine hydroxylation and its subsequent decarboxylation to produce succinate.

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Glycine synthesis

The formation of glycine from different precursors, including glyoxylate and glutamate, or alanine.

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Transamination of Pyruvate

A reaction that converts pyruvate into alanine using a specific aminotransferase enzyme.

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Transamination of Oxaloacetate

The conversion of oxaloacetate into aspartate through a transamination reaction.

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Chole and Serine's role in Glycine Formation

Other important pathways for forming glycine originate from choline and serine.

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Glutamine synthetase

An enzyme catalyzing the reaction of glutamate to glutamine.

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Asparagine synthetase

Enzyme catalyzing aspartate to asparagine.

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Aminotransferases

Enzymes that catalyze the transfer of an amino group from one molecule to another.

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Alanine

An amino acid formed from pyruvate in transamination reactions.

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Aspartate

An amino acid synthesized from oxaloacetate through transamination.

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Tyrosine biosynthesis

Tyrosine is synthesized from phenylalanine.

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Essential amino acid

An amino acid that the body cannot produce and must obtain from food.

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Nonessential amino acid

An amino acid that the body can produce.

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Tyrosine's status

Tyrosine is considered semi-essential, meaning the body can make it, but may need dietary intake during certain stages like growth.

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Collagen production

Tyrosine is involved in collagen synthesis (post-translational modification).

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Aminotransferases

Enzymes involved in amino acid biosynthesis, particularly in incorporating toxic ammonium.

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Glutamate dehydrogenase

Enzyme central to converting potentially toxic ammonium ion into non-toxic amino acids.

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Glutamine synthetase

An enzyme that plays a part in incorporating potentially toxic ammonium ion, transforming it into a non-toxic amino acid.

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Biosynthesis of nonessential amino acids

Involves the combined action of glutamate dehydrogenase, glutamine synthetase, and aminotransferases.

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Nutritional value of amino acids

The degree to which amino acids are essential or not depends on the rates your body makes them

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Glutamate Formation

Glutamate is formed by reductive amidation of α-ketoglutarate, facilitated by mitochondrial glutamate dehydrogenase.

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Glutamine Synthesis

Glutamine is synthesized from glutamate by amidation, involving γ-glutamyl phosphate as an intermediate, catalyzed by glutamine synthetase.

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Asparagine Synthesis

Asparagine is formed from aspartate, using glutamine as a nitrogen source, catalyzed by asparagine synthetase.

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3-Phosphoglycerate to Serine

Serine is generated through the oxidation of 3-phosphoglycerate, a glycolytic intermediate.

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γ-glutamyl phosphate

An intermediate in the synthesis of glutamine, formed when glutamate reacts with ATP.

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Proline Biosynthesis

The process of creating proline from glutamate, involving several enzymatic steps, including reduction and cyclization.

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Cysteine Formation

Cysteine synthesis from methionine, a precursor, via homocysteine and cystathionine.

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Tyrosine Synthesis

Tyrosine production from the essential amino acid phenylalanine, if enough phenylalanine is available in the diet.

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Hydroxyproline and Hydroxylysine

Amino acids found primarily in collagen, not directly incorporated during protein synthesis because there is no corresponding tRNA.

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Phenylalanine Hydroxylase

Enzyme catalyzing the conversion of phenylalanine to tyrosine, incorporating oxygen and generating water.

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Scurvy

A nutritional disorder caused by vitamin C deficiency, leading to weakened collagen and various health problems.

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Amino acid deficiency

Results from an inadequate intake of essential amino acids in the diet, or from genetic disorders impacting their synthesis.

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Kwashiorkor

A nutritional disorder, often seen in children, arising from a low protein diet, especially when weaning onto starchy foods.

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Marasmus

A nutritional disorder resulting from a deficiency in both calories and specific amino acids.

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Menkes syndrome

A genetic disorder caused by a copper deficiency, affecting collagen formation and other metabolic processes.

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Essential amino acid

An amino acid the body cannot produce and must obtain from diet.

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Collagen

A structural protein important for connective tissues, whose strength relies on specific cross-links.

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Short bowel syndrome

A condition where the small intestine cannot absorb enough nutrients.

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Nutritional Essential Amino Acids

Amino acids the body cannot create and must receive from food

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Biosynthesis of Nutritionally Essential Amino Acids

Metabolic processes forming essential amino acids, usually lengthy and complex.

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Essential Amino Acids

Amino acids the body cannot produce and must be obtained from food.

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Nonessential Amino Acids

Amino acids the body can produce.

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Amino Acid Deficiency

When the body lacks sufficient amounts of specific amino acids, leading to health problems.

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Kwashiorkor

A nutritional disorder caused by inadequate protein intake, often when a child is weaned to a starchy diet.

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Marasmus

A nutritional disorder caused by a deficiency in both caloric intake and specific amino acids.

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Biosynthesis of Amino Acids

The process of creating amino acids from other molecules within the body.

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Tryptophan & Lysine Deficiency

Diets heavily relying on grains, particularly in West Africa, may result in Tryptophan and Lysine deficiency leading to nutritional problems.

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Number of Enzymes

Different numbers of enzymes are required to synthesize essential and non-essential amino acids.

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Proline Biosynthesis

The process of creating proline from glutamate, involving enzymatic steps like reduction and cyclization.

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Cysteine Formation

Synthesized from methionine, a precursor, through homocysteine and cystathionine.

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Tyrosine Synthesis

Produced from phenylalanine if sufficient phenylalanine is in the diet.

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Hydroxyproline/Hydroxylysine

Amino acids primarily in collagen, not incorporated directly during protein synthesis due to lack of corresponding tRNA.

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Phenylalanine Hydroxylase

Enzyme converting phenylalanine to tyrosine, involving oxygen incorporation.

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3-Phosphoglycerate to Serine

Serine is generated from the glycolytic intermediate 3-phosphoglycerate via oxidation.

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Glutamate Formation

Glutamate is created from α-ketoglutarate through a reductive amidation reaction, facilitated by mitochondrial glutamate dehydrogenase.

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Glutamine Synthesis

Glutamine is formed from glutamate through an amidation reaction, using γ-glutamyl phosphate as an intermediate and catalyzed by glutamine synthetase.

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Asparagine Synthesis

Asparagine is created from aspartate, using glutamine as a nitrogen source, and is catalyzed by asparagine synthetase.

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3-Phosphoglycerate to Serine

Serine is produced from the oxidation of the glycolytic intermediate 3-phosphoglycerate, which forms 3-phosphohydroxypyruvate.

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γ-glutamyl phosphate

An intermediate in glutamine synthesis, formed when glutamate reacts with ATP.

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Glutamate dehydrogenase

The enzyme crucial for converting potentially toxic ammonium ions into the non-toxic amino acid glutamate.

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Glutamine synthetase

An enzyme catalyzing the conversion of glutamate to glutamine.

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Asparagine synthetase

Enzyme catalyzing aspartate to asparagine.

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Successive enzyme-catalyzed reactions

A series of reactions using enzymes to transform one molecule into another, specifically changing cysteine-tRNA to selenocysteine-tRNA.

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Selenocysteine incorporation

Selenocysteine, the 21st amino acid, is added into proteins in the presence of a specific elongation factor.

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Mixed-function oxidase

An enzyme type that incorporates molecular oxygen into a molecule, like proline or succinate, in a multi-step reaction.

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Procollagen-proline 4-hydroxylase

A specific enzyme (EC 1.14.11.2) that catalyzes the hydroxylation of proline in collagen.

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Selenoproteins

Proteins containing selenocysteine.

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α-keto acids

Can replace their corresponding amino acids in the diet, meaning body makes them.

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Scurvy impact

Vitamin C deficiency prevents proper hydroxylation of proline and lysine, hindering collagen cross-linking and causing weakened collagen, leading to poor wound healing and general issue.

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Phenylalanine hydroxylase

Enzyme that converts phenylalanine to tyrosine.

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Nonessential Amino Acids

Amino acids the body can produce.

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Essential Amino Acids

Amino acids the body cannot produce, must be obtained from food.

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Amino Acid Biosynthesis

The process of creating amino acids within the body.

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Transamination

Transferring an amino group from one molecule to another.

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Scurvy Cause

Vitamin C deficiency leading to a collagen weakness issue.

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Selenocysteine's Role

An essential component of some mammalian proteins.

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Mixed-Function Oxidase

Enzyme incorporating oxygen into a molecule.

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Tetrahydrobiopterin's Role

Helps in the synthesis of tyrosine.

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Modified tRNA

Facilitates the insertion of selenocysteine in proteins.

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Collagen Hydroxylation

Modification of proline and lysine in collagen, requiring Vitamin C.

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Nutritionally Essential Amino Acids

Amino acids the body needs but cannot produce, requiring intake from food.

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Nutritionally Nonessential Amino Acids

Amino acids the body can produce itself.

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Essential vs. Nonessential Confusion

While the terms "essential" and "nonessential" are used with amino acids, all 20 amino acids are essentially essential for human health.

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8 Nutritionally Essential Amino Acids

Eight amino acids that humans must get from their diet unlike the other 12 that can be synthesized in the body.

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Dietary Amino Acid Replacement

Substituting purified amino acids for protein in a diet to distinguish essential and nonessential amino acids.

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Biosynthesis of Amino Acids

Process by which organisms, other than humans, create certain amino acids.

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Study Notes

Amino Acid Metabolism

  • Certain amino acids are not essential for human health.
  • Essential vs Nutritionally essential amino acids are different.
    • 8 amino acids are nutritionally essential for humans.
    • 12 nutritionally non-essential amino acids can be synthesized metabolically.
  • The citric acid cycle and glycolysis intermediates are precursors for some amino acids (aspartate, asparagine, glutamate, glutamine, glycine, and serine).
  • Transaminases play a key role in amino acid metabolism.
  • 4-hydroxyproline and 5-hydroxylysine are formed in proteins like collagen.
  • Vitamin C deficiency (scurvy) impacts collagen formation.
  • Selenium, despite being toxic, is essential for selenocysteine, a component of some proteins.
  • A mixed-function oxidase is defined and its role in some reactions is outlined.
  • Tetrahydrobiopterin is a crucial component in tyrosine biosynthesis.
  • Modified tRNA is involved in selenocysteine insertion during protein synthesis.

Biomedical Importance of Amino Acids

  • Amino acid deficiencies can arise from inadequate intake or absorption.
  • Kwashiorkor and marasmus are nutritional disorders caused by deficiencies.
  • Short bowel syndrome can lead to nutritional issues for patients.
  • Genetic disorders affect the formation of hydroxyproline and hydroxylysine in collagen.
  • Menkes syndrome, linked to a copper deficiency, affects collagen structure.

Biosynthesis of Nonessential Amino Acids

  • Glutamate is derived from a-ketoglutarate via glutamate dehydrogenase.
  • Glutamine synthesis involves glutamine synthetase and y-glutamyl phosphate as intermediates.
  • Alanine and aspartate biosynthesis are via transamination of pyruvate and oxaloacetate, respectively.
  • Asparagine synthesizes via glutamines production.
  • Serine is formed by oxidation of 3-phosphoglycerate, via transamination and dephosphorylation
  • Glycine synthesis uses glyoxylate, glutamate, or alanine via aminotransferases.
  • Proline synthesis follows a pathway with glutamate y-semialdehyde as a crucial intermediate.
  • Cysteine is synthesized from methionine, with homocysteine and serine as intermediates.
  • Tyrosine production from phenylalanine requires phenylalanine hydroxylase.
  • Hydroxyproline and hydroxylysine's biosynthesis are specific to collagen.
  • The hydroxylases require vitamin C and molecular oxygen.
  • Valine, leucine, and isoleucine are interconverted by tissue aminotransferases.

Selenocysteine

  • Selenocysteine (21st nonessential amino acid) is found in some proteins.
  • It's a crucial part of some enzymes involved in redox reactions.
  • Selenocysteine biosynthesis involves serine, selenate, ATP, specific tRNA (tRNASec), and multiple enzymes.
  • The selenocysteine insertion element (stem-loop in mRNA) guides correct incorporation.

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