BIOC 3110 Lecture Notes - Lecture 30: Glutamine Synthetase, Carbamoyl Phosphate, Glutamate Dehydrogenase
13 Nov 2016
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Lecture 30: amino acid degradation + urea cycle. Proteins and cellular proteins are degraded to amino acids. Do cells have a storage form for excess amino acids: cells make aa and digest them, but, they have no storage form of them, they must break them down as soon as acquired, because nitrogen is toxic. What is the role of aminotransferases (aka transaminoases): 1. Transfer an nh3 from aa to alpha-ketoglutarate to make glutamate: this enzyme is reversible; can be used in synthesis of aa, overall initial step: aa + alpha-ketoglutarate glutamate by aminotransferase, ex. The keto acids enter the citric acid cycle, and glutamine is. Role of glutamate dehydrogenases? further degraded: breaks down glutamine and removes nitrogen, 2. glutamine + nad+/nadp+ alpha ketoglutarate + nh4 by glutamate dehydrogenase in mitochondria. The nh3 is released in mitochondria of liver to limit toxicity. This enzyme is stimulated by high levels of adp and gdp, aka.
