BIOC 3300 Lecture Notes - Lecture 20: Glutamine Synthetase, Glutamate Dehydrogenase, Nitrogen Fixation

• School: Dalhousie University
• Department: Biochem & Molecular Biology
• Course: BIOC 3300
• Professor: Mc Leod Roger

Document Summary

Lecture 20 - nitrogen fixation and ammonia assimilation. N-n triple bond is a very high energy bond (940 kj/mol: why does biological nitrogen fixation require so much energy, does nitrogen anaerobic. Mofe-protein - component i, nitrogenase, tetrameric structure, has 4 redox centers. [nh4] be low or high: glutamine synthetase: Substrate: -ketoglutarate reversible reaction cofactor: nadph (more common in plants) or nadh (more commonly used in the mitochondrial glutamate dehydrogenase in glutamine degradation) Low [nh4] gives maximum reaction rates (opposite of glutamate dehydrogenase) Amide nitrogen becomes -amino n in the synthesis of other amino acids, along with purines and pyrimidines ratio of -ketoglutarate to glutamine, and. [nh4] promote uridylylation of adenylyltransferase, which itself promotes deadenylation of glutamine synthetase tyr residue, making it more active. Causes de-uridylylation of adenylyltransferase and adenylation of glutamine synthetase (making it more active: what is the more active and less active states of glutamine synthetase, what is the result of .