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Transaminases
Class of enzymes that catalyze the exchange of amino groups between α-amino acids and α-keto acids.
Deamination
The removal of an amino group from an amino acid, resulting in the formation of an α-keto acid.
Reductive Amination
A reaction catalyzed by Glutamate Synthase that transfers amido nitrogen from glutamine to α-ketoglutarate to generate glutamate.
Glutamate
An α-amino acid that serves as a primary nitrogen donor in amino group transfers.
α-Keto Acid
Organic compounds containing a keto group adjacent to a carboxyl group, often serving as acceptors of amino groups.
Amino Group
A functional group that, when transferred, converts α-keto acids into α-amino acids.
Aspartate
An α-amino acid derived from oxaloacetate via transaminase reaction.
Serine
An α-amino acid that can be synthesized from 3-phosphoglycerate in a few steps.
Urea Cycle
The biochemical pathway through which ammonia is converted into urea for detoxification.
Glucogenic Amino Acids
Amino acids that can be converted into glucose through gluconeogenesis.
Ketogenic Amino Acids
Amino acids that can be converted into ketone bodies or acetyl CoA for energy production.
Transaminases catalyze the exchange of __________ between α-amino acids and α-keto acids.
amino groups
The process of removing an amino group from an amino acid is known as __________.
deamination
__________ is a reaction that transfers amido nitrogen from glutamine to α-ketoglutarate.
Reductive amination
Glutamate serves as a primary nitrogen donor in __________ group transfers.
amino
An __________ is an organic compound containing a keto group adjacent to a carboxyl group.
α-keto acid
The functional group that converts α-keto acids into α-amino acids is called an __________ group.
amino
Aspartate is derived from __________ via a transaminase reaction.
oxaloacetate
__________ can be synthesized from 3-phosphoglycerate in a few steps.
Serine
The __________ pathway converts ammonia into urea for detoxification.
Urea Cycle
Glucogenic amino acids can be converted into __________ through gluconeogenesis.
glucose
The main function of transaminases is to facilitate the transfer of __________ groups.
amino
The formation of urea occurs mainly in the __________ and is part of the urea cycle.
liver
The amino acid __________ can be synthesized from pyruvate through transamination.
alanine
In deamination, the amino group is typically converted to __________ for excretion.
ammonia
__________ is the starting point for the synthesis of non-essential amino acids.
α-keto acid
The process of converting phenylalanine to tyrosine is an example of __________.
hydroxylation
In the urea cycle, __________ is combined with carbon dioxide to form carbamoyl phosphate.
ammonia
The side chain of the amino acid __________ contains a sulfur atom and can form disulfide bonds.
cysteine
Amino acids can act as precursors for the synthesis of __________ neurotransmitters like serotonin.
biogenic
The amino acid __________ can be both glucogenic and ketogenic depending on metabolic pathway.
isoleucine
During fasting, the body can convert __________ acids into glucose through gluconeogenesis.
glucogenic
__________ is synthesized from the amino acid serine and is essential for DNA methylation.
S-adenosylmethionine
The conversion of kynurenine to __________ is a step in tryptophan metabolism.
niacin
Amino acids are linked together by __________ bonds to form proteins.
peptide
The branch chain amino acids include leucine, isoleucine, and __________.
valine
The only amino acid that is a primary amino acid and not a secondary is __________.
glycine
The enzyme __________ catalyzes the reaction of α-ketoglutarate to form glutamate.
glutamate dehydrogenase
__________ amino acids are those that the body cannot synthesize and must be obtained from the diet.
Essential
Glutamine serves as a nitrogen donor in the synthesis of __________.
nucleotides
__________ is the metabolic state in which amino acids are primarily used for energy production.
Fasting