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Chapter 17 - Amino Acid Metabolism Metabolism of the 20 common amino acids is considered from the origins and fates of their: (1) Nitrogen atoms (2) Carbon.

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Presentation on theme: "Chapter 17 - Amino Acid Metabolism Metabolism of the 20 common amino acids is considered from the origins and fates of their: (1) Nitrogen atoms (2) Carbon."— Presentation transcript:

1 Chapter 17 - Amino Acid Metabolism Metabolism of the 20 common amino acids is considered from the origins and fates of their: (1) Nitrogen atoms (2) Carbon skeletons For mammals: Essential amino acids must be obtained from diet Nonessential amino acids - can be synthesized

2 17.1 The Nitrogen Cycle and Nitrogen Fixation Nitrogen is needed for amino acids, nucleotides Atmospheric N 2 is the ultimate source of biological nitrogen Nitrogen fixation: a few bacteria possess nitrogenase which can reduce N 2 to ammonia Nitrogen is recycled in nature through the nitrogen cycle

3 Fig 17.1 The Nitrogen cycle

4 Nitrogenase An enzyme present in Rhizobium bacteria that live in root nodules of leguminous plants Some free-living soil and aquatic bacteria also possess nitrogenase Nitrogenase reaction: N H e ATP 2 NH 3 + H ADP + 16 P i

5 17.2 Assimilation of Ammonia Ammonia generated from N 2 is assimilated into low molecular weight metabolites such as glutamate or glutamine At pH 7 ammonium ion predominates (NH 4 + ) At enzyme reactive centers unprotonated NH 3 is the nucleophilic reactive species

6 A. Ammonia Is Incorporated into Glutamate Reductive amination of  -ketoglutarate by glutamate dehydrogenase occurs in plants, animals and microorganisms In mammals & plants, located in mitochondria.

7 B. Glutamine Is a Nitrogen Carrier in Many Biosynthetic Reactions A second important route in assimilation of ammonia is via glutamine synthetase

8 Glutamate synthase transfers a nitrogen to  -ketoglutarate Prokaryotes & plants

9 Fig 17.3 Alternate amino acid production in prokaryotes Especially used if [NH 3 ] is low. K m of Gln synthetase lower than K m of Glu dehydrogenase.

10 Box 17.1 How some enzymes transfer ammonia from glutamine CP synthetase has 3 active sites connected by a tunnel running through the interior Protects intermediates from being degraded by water

11 Carbamoyl phosphate synthase backbone structure Tunnel connecting active sites (blue wire)

12 C. Regulation of Glutamine Synthetase in E. coli Glutamine synthetase (GS) plays a critical role in nitrogen metabolism E. coli enzyme regulated by: (1) Cumulative feedback inhibition (9 allosteric inhibitors with additive effects) (2) Covalent modification (3) Regulation of enzyme synthesis

13 Fig 17.4 Allosteric inhibition of GS in E. coli

14 Fig 17.5 Regulation of E. coli GS by covalent modification

15 Regulation of mammalian GS Regulation not as extensive as in microorganisms No covalent regulation Allosteric inhibitors: glycine, serine, alanine, and carbamoyl phosphate Allosteric activator:  -ketoglutarate

16 17.3 Transamination Reactions Transfer of an amino group from an  -amino acid to an  -keto acid In amino acid biosynthesis, the amino group of glutamate is transferred to various  -keto acids generating  -amino acids In amino acid catabolism, transamination reactions generate glutamate or aspartate

17 Fig 17.6 Transamination reactions

18 Fig 17.7 Ping-pong kinetics of aspartate transaminase (next slide)

19 Fig 17.7 (cont) (from previous slide)


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