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Questions and Answers
Which category of amino acids contains a benzene ring or a nonbenzene hydrocarbon chain?
Which category of amino acids contains a benzene ring or a nonbenzene hydrocarbon chain?
Which amino acid contains a thiol group that can form disulfide bonds?
Which amino acid contains a thiol group that can form disulfide bonds?
Which amino acid is sometimes grouped with neutral polar amino acids, despite being borderline with respect to polarity?
Which amino acid is sometimes grouped with neutral polar amino acids, despite being borderline with respect to polarity?
Which amino acid can be phosphorylated and has an OH group that can be a site of carbohydrate attachment?
Which amino acid can be phosphorylated and has an OH group that can be a site of carbohydrate attachment?
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Which category of amino acids has a negative charge and is hydrophilic?
Which category of amino acids has a negative charge and is hydrophilic?
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Which category of amino acids has a positive charge and is hydrophilic?
Which category of amino acids has a positive charge and is hydrophilic?
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Which amino acid is not commonly found in protein structures that require rotation, such as alpha-helices?
Which amino acid is not commonly found in protein structures that require rotation, such as alpha-helices?
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Which amino acid contains sulfur and can help bind metals?
Which amino acid contains sulfur and can help bind metals?
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Which amino acid is part of many important proteins and peptides, including keratin and insulin?
Which amino acid is part of many important proteins and peptides, including keratin and insulin?
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Which amino acid is an antioxidant, with the sequence Gly-Cys-Glu?
Which amino acid is an antioxidant, with the sequence Gly-Cys-Glu?
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Which of the following is NOT one of the three ways nitrogen can be incorporated into an amino acid?
Which of the following is NOT one of the three ways nitrogen can be incorporated into an amino acid?
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Which coenzyme is required for transaminations to occur?
Which coenzyme is required for transaminations to occur?
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Which enzyme is responsible for the conversion of glutamate to glutamine in the glutamate family of amino acids?
Which enzyme is responsible for the conversion of glutamate to glutamine in the glutamate family of amino acids?
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Which amino acid family shares pyruvate as a common precursor?
Which amino acid family shares pyruvate as a common precursor?
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Which amino acid is synthesized directly from pyruvate?
Which amino acid is synthesized directly from pyruvate?
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What is the coenzyme form of vitamin B9 (folate) that picks up the nitrogen during serine metabolism?
What is the coenzyme form of vitamin B9 (folate) that picks up the nitrogen during serine metabolism?
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What can a deficiency in folate lead to?
What can a deficiency in folate lead to?
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Can supplementing with folate decrease the likelihood of certain cancers?
Can supplementing with folate decrease the likelihood of certain cancers?
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Would it be good or bad to supplement with folate if someone already has cancer?
Would it be good or bad to supplement with folate if someone already has cancer?
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Which amino acid family includes histidine?
Which amino acid family includes histidine?
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Which of the following is a symptom of Phenylketonuria (PKU)?
Which of the following is a symptom of Phenylketonuria (PKU)?
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What is the significance of histamine in the body?
What is the significance of histamine in the body?
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Where does the urea cycle occur in the body?
Where does the urea cycle occur in the body?
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Which molecule is used to start the urea cycle?
Which molecule is used to start the urea cycle?
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Where does the nitrogen for urea come from?
Where does the nitrogen for urea come from?
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Which amino acids are both glucogenic and ketogenic?
Which amino acids are both glucogenic and ketogenic?
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Which amino acid can be decarboxylated to produce histamine?
Which amino acid can be decarboxylated to produce histamine?
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What is the purpose of the urea cycle?
What is the purpose of the urea cycle?
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Which enzyme is responsible for the conversion of arginine to ornithine in the urea cycle?
Which enzyme is responsible for the conversion of arginine to ornithine in the urea cycle?
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Which part of the body has high levels of glutamine synthetase?
Which part of the body has high levels of glutamine synthetase?
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Which amino acid family contains amino acids with a negative charge and is hydrophilic?
Which amino acid family contains amino acids with a negative charge and is hydrophilic?
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Which amino acid family contains amino acids with a positive charge and is hydrophilic?
Which amino acid family contains amino acids with a positive charge and is hydrophilic?
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Which amino acid family contains amino acids with a benzene ring or a nonbenzene hydrocarbon chain?
Which amino acid family contains amino acids with a benzene ring or a nonbenzene hydrocarbon chain?
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Which amino acid family contains amino acids with a hydroxyl group that can be a site of carbohydrate attachment?
Which amino acid family contains amino acids with a hydroxyl group that can be a site of carbohydrate attachment?
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Which amino acid contains a thiol group that can form disulfide bonds?
Which amino acid contains a thiol group that can form disulfide bonds?
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Which amino acid is sometimes grouped with neutral polar amino acids, despite being borderline with respect to polarity?
Which amino acid is sometimes grouped with neutral polar amino acids, despite being borderline with respect to polarity?
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Which amino acid is part of many important proteins and peptides, including keratin and insulin?
Which amino acid is part of many important proteins and peptides, including keratin and insulin?
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Which amino acid can be phosphorylated and has an OH group that can be a site of carbohydrate attachment?
Which amino acid can be phosphorylated and has an OH group that can be a site of carbohydrate attachment?
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Which amino acid is not commonly found in protein structures that require rotation, such as alpha-helices?
Which amino acid is not commonly found in protein structures that require rotation, such as alpha-helices?
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Which amino acid contains a sulfur atom and can help bind metals?
Which amino acid contains a sulfur atom and can help bind metals?
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Which of the following is NOT a way that nitrogen can be incorporated into an amino acid?
Which of the following is NOT a way that nitrogen can be incorporated into an amino acid?
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Which of the following amino acids is part of the pyruvate family?
Which of the following amino acids is part of the pyruvate family?
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Which enzyme is responsible for the conversion of glutamate to glutamine in the glutamate family of amino acids?
Which enzyme is responsible for the conversion of glutamate to glutamine in the glutamate family of amino acids?
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Which amino acid is both glucogenic and ketogenic?
Which amino acid is both glucogenic and ketogenic?
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Which category of amino acids contains a benzene ring or a nonbenzene hydrocarbon chain?
Which category of amino acids contains a benzene ring or a nonbenzene hydrocarbon chain?
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What is the purpose of the urea cycle?
What is the purpose of the urea cycle?
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Which molecule is used to start the urea cycle?
Which molecule is used to start the urea cycle?
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Which amino acid family includes histidine?
Which amino acid family includes histidine?
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Which amino acid is an antioxidant, with the sequence Gly-Cys-Glu?
Which amino acid is an antioxidant, with the sequence Gly-Cys-Glu?
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Which part of the body has high levels of glutamine synthetase?
Which part of the body has high levels of glutamine synthetase?
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Which amino acid is both glucogenic and ketogenic?
Which amino acid is both glucogenic and ketogenic?
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Which amino acid is involved in the synthesis of the important electron carrier CoQ in animals?
Which amino acid is involved in the synthesis of the important electron carrier CoQ in animals?
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Which amino acid is associated with the autosomal recessive disorder Phenylketonuria (PKU)?
Which amino acid is associated with the autosomal recessive disorder Phenylketonuria (PKU)?
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Which amino acid is converted to phenylketone and excreted in urine in individuals with Phenylketonuria (PKU)?
Which amino acid is converted to phenylketone and excreted in urine in individuals with Phenylketonuria (PKU)?
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Which amino acid is part of the aromatic family and is only found in plants?
Which amino acid is part of the aromatic family and is only found in plants?
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Which amino acid can be decarboxylated to produce histamine?
Which amino acid can be decarboxylated to produce histamine?
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Which amino acid is an important precursor for the synthesis of neurotransmitters such as dopamine and norepinephrine?
Which amino acid is an important precursor for the synthesis of neurotransmitters such as dopamine and norepinephrine?
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Which enzyme is responsible for the conversion of arginine to ornithine in the urea cycle?
Which enzyme is responsible for the conversion of arginine to ornithine in the urea cycle?
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Where does the urea cycle occur in the body?
Where does the urea cycle occur in the body?
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What is the purpose of the urea cycle?
What is the purpose of the urea cycle?
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Study Notes
Amino Acid Categories
- Aromatic amino acids contain a benzene ring or a nonbenzene hydrocarbon chain
- Acidic amino acids have a negative charge and are hydrophilic
- Basic amino acids have a positive charge and are hydrophilic
Amino Acid Properties
- Cysteine contains a thiol group that can form disulfide bonds
- Tyrosine is sometimes grouped with neutral polar amino acids, despite being borderline with respect to polarity
- Serine can be phosphorylated and has an OH group that can be a site of carbohydrate attachment
- Glycine is not commonly found in protein structures that require rotation, such as alpha-helices
- Methionine contains sulfur and can help bind metals
- Cysteine is part of many important proteins and peptides, including keratin and insulin
Amino Acid Families
- Glutamate family shares pyruvate as a common precursor
- Aspartate family includes aspartate and asparagine
- Histidine family includes histidine
- Pyruvate family includes alanine, valine, and leucine
Urea Cycle
- Occurs in the liver and kidney
- Purpose is to remove ammonia from the body
- Starts with the molecule ammonia
- Nitrogen for urea comes from ammonia
- Arginine is converted to ornithine in the urea cycle by the enzyme ornithine transcarbamylase
- Ornithine is then converted to citrulline
Other Amino Acids
- Glutamine is an important precursor for the synthesis of neurotransmitters such as dopamine and norepinephrine
- Phenylalanine is associated with the autosomal recessive disorder Phenylketonuria (PKU)
- Tyrosine can be decarboxylated to produce histamine
- Glutamine synthetase is found in high levels in the brain
Vitamin B9 (Folate)
- Coenzyme form is tetrahydrofolate (THF)
- Picks up nitrogen during serine metabolism
- Deficiency in folate can lead to anemia and birth defects
- Supplementing with folate can decrease the likelihood of certain cancers
- However, it is not recommended to supplement with folate if someone already has cancer
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Description
Test your knowledge of amino acid classifications! This quiz will challenge you to categorize amino acids based on their polarity, describe the properties of each category, and identify any unique groups. Can you match the 3-letter and 1-letter codes to the correct amino acids? Put your skills to the test with this amino acid classification quiz!