Notes in e. Nitrogen and Amino Acid Metabolism

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Published	07/28/2024	The {{c1::liver}} is the primary site for amino acid degradation though under some conditions, {{c1::muscle}} can degrade branched chain amino ac…
Published	07/28/2024	{{c1::Nitrogen balance}} is the measure of balance between protein intake and degradation
Published	07/28/2024	A {{c1::positive}} nitrogen balance occurs durring child growth
Published	07/28/2024	A {{c1::positive}} nitrogen balance occurs during pregnancy
Published	07/28/2024	A {{c1::positive}} nitrogen balance occurs during healing
Published	07/28/2024	A {{c1::positive}} nitrogen balance occurs during muscle building
Published	07/28/2024	A {{c1::positive}} nitrogen balance occurs during refeeding after starvation
Published	07/28/2024	A {{c1::negative}} nitrogen balance occurs during illness
Published	07/28/2024	A {{c1::negative}} nitrogen balance occurs during starvation
Published	07/28/2024	A {{c1::negative}} nitrogen balance occurs during trauma
Published	07/28/2024	A {{c1::negative}} nitrogen balance occurs in a diet deficient in essential amino acids
Published	07/28/2024	{{c1::Non-essential}} amino acids can be synthesized de novo
Published	07/28/2024	{{c1::Essential}} amino acids must be obtained from the diet
Published	07/28/2024	In {{c3::muscle}}, {{c1::pyruvate}} is the preferred nitrogen acceptor for glutamate transaminations, yielding {{c2::alanine}}. This enzyme …
Published	07/28/2024	In tissues including the {{c1::liver}}, {{c2::alpha-ketogluturate}} is the preferred nitrogen acceptor in transaminations from aspartate, yi…
Published	07/28/2024	Aminotransferases typically uses {{c1::PLP}} a {{c2::Vitamin B6}} derivative as a cofactor
Published	07/28/2024	How can alanine aminotransferase and aspartate aminotransferase be used in liver function tests?
Published	07/28/2024	{{c1::Glutamate Dehydrogenase}} is a key enzyme in amino acid catabolism that removes an amino group from glutamate, releases it as ammonium, and prod…
Published	07/28/2024	Glutamate dehydrogenase is found in the {{c1::liver}} and {{c2::kidney}} and important for release of {{c1::free ammonia}}
Published	07/28/2024	{{c1::Serine Dehydratase}} removes {{c1::ammonia}} from serine, to produce {{c2::pyruvate}}
Published	07/28/2024	Ammonium is removed from asparagine by the enzyme {{c1::asparaginase}}
Published	07/28/2024	Ammonium is removed from glutamine by the enzyme {{c1::glutaminase}} which produces glutamate. The reverse reaction is catalyzed by {{c1::glutami…
Published	07/28/2024	What are the 2 methods by which ammonium is transported in the blood?
Published	07/28/2024	Explain how ammonium can be transported in the blood via glutamine.
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Published	07/28/2024	The urea cycle occurs in the {{c1::liver}}, glutamate dehydrogenase or glutaminase provide {{c1::NH4+}}, aspartate provides other {{c1::NH4+}}, {…
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Published	07/28/2024	Carbamoyl phosphate synthesis I occurs in the {{c1::mitochondrial matrix}}. If it is defective that causes build up of {{c1::ammonia}}
Published	07/28/2024	Carbomyl Phosphate synthesis requires {{c1::2}} ATP
Published	07/28/2024	{{c1::Carbamoyl phosphate synthase I}} is the {{c1::first}} step in the urea cycle and is responsible for synthesizing carbamoyl phosphate
Published	07/28/2024	Citrulline synthesis occurs in the {{c1::mitochondrial matrix}} because it is formed in the {{c1::second}} step of the {{c1::urea}} cycle
Published	07/28/2024	{{c1::Ornithine transcarbamoylase}} (step 2 of the urea cycle) is the enzyme responsible for synthesizing citrulline from ornithine and carbomyl phosp…
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Published	07/28/2024	Carbamoyl phosphate synthetase I takes place in {{c1::mitochondrial matrix}}, is allosterically {{c1::activated}} by {{c1::NAG (N-acetyl glutamat…
Published	07/28/2024	{{c1::Carbamoyl Phosphate Synthase I}} is the rate limiting step of the Urea Cycle because it is irreversible and costs 2 ATP
Published	07/28/2024	Ammonium is very toxic to the {{c1::CNS}}
Published	07/28/2024	Urea cycle defects are caused by loss of an enzyme function, ultimately causing toxic buildup of {{c1::ammonium}} because the purpose of the urea…
Published	07/28/2024	In the case of an arginosuccinase (argine lyase) deficiency, {{c1::arginine}} can be administered in stoichiometric quantities, which allows for …
Published	07/28/2024	What is the inheritance pattern of OTCD? What is built up in the mitochondria as a result? How can benzoate and phenylacetate be used for treatment of…
Published	07/28/2024	{{c1::Glucogenic}} amino acids have carbon backbones that can be converted into glucose
Published	07/28/2024	{{c1::Ketogenic}} amino acids have carbon backbones that can be converted into acetyl CoA and ketone bodies. Because Acetyl CoA cannot be converted ba…
Published	07/28/2024	{{c1::Maple syrup urine disease}} is due to a genetic defect in branched-chain alpha-keto acid dehydrogenase, an enzyme critical in the metabolism of …
Published	07/28/2024	{{c1::Tyrosine}} is the starting point for synthesis of catecholamines (dopamine, norep/ep). One of the reasons to give {{c1::tyrosine}} to {{c1::PKU}…
Published	07/28/2024	{{c1::Tryptophan}} is the starting point in the synthesis of serotonin
Published	07/28/2024	{{c1::Glutamate}} is the starting point in the synthesis of GABA
Published	07/28/2024	{{c1::Histidine}} is the starting point in the synthesis of histamine
Published	07/28/2024	How are urea cycle defects diagnosed?
Published	07/28/2024	How are urea cycle defects managed?
Published	07/28/2024	What are general pathways of deaminating glucogenic acids for their use in glucose synthesis
Published	07/28/2024	What are the important aspects of Phenylketonuria and how is caused/treated?
Published	07/28/2024	Other important products made from amino acids
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