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Section M Nitrogen metabolism 1. Reduction of N 2 into ammonia (NH 3 or NH 4 + ) 2. Synthesis of the 20 amino acids. 3. Amino acid degradation.

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Presentation on theme: "Section M Nitrogen metabolism 1. Reduction of N 2 into ammonia (NH 3 or NH 4 + ) 2. Synthesis of the 20 amino acids. 3. Amino acid degradation."— Presentation transcript:

1 Section M Nitrogen metabolism 1. Reduction of N 2 into ammonia (NH 3 or NH 4 + ) 2. Synthesis of the 20 amino acids. 3. Amino acid degradation

2 M1 Nitrogen fixation and assimilation The nitrogen cycle Nitrogen fixation Nitrogen assimilation

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4 The nitrogen in amino acids, purines, pyrimidines and other biomolecules ultimately comes from atmospheric nitrogen. Cyanobacteria (, photosynthetic) and rhizobia (, symbiont) can fix N 2 into NH 3. The reduction of N 2 to NH 3 is thermodynamically favorable : N 2 + 6e - + 6H + 2NH 3 G` o = -33.5kJ/mol

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6 Certain bacteria can fix N 2 into ammonia N 2 + 6e - + 6H + 2NH 3 G` o = kJ/mol

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8 The nitrogenase complex in certain bacteria catalyzes the conversion of N 2 to NH 3, which is the ultimate source of nitrogen for all the nitrogen-containing biomolecules.

9 The nitrogenase complex consists of dinitrogenase and dinitrogenase redutase ADP 4Fe-4S (P-cluster) Fe-Mo cofactor e-e- ? 4Fe-4S (P-cluster) 4Fe-4S ADP

10 Molybdenum N 2 is believed to be reduced at the Fe-Mo cofactor N2N2 Fe S S S S S S S S S Mo

11 Electrons are transferred through a series of carriers to N 2 for its reduction on the nitrogenase complex N 2 + 8H+ +8e- + 16ATP + 16H 2 O 2NH 3 + H ADP + 16P i

12 Electrons are transferred to N 2 bound in the active site of dinitrogenase via ferredoxin/ flavodoxin and dinitrogenase reductase

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14 Reduced nitrogen in the form of NH 4 + is assimilated into organic nitrogen- containing compounds by the action of glutamate dehydrogenase and glutamine synthetase. Ammonia is incorporated into biomolecules through Glutamate and glutamine.

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16 glutamate dehydrogenase

17 glutamine synthetase

18 Glutamate + NH 3 +ATP Glutamine + ADP + Pi Glutamine + Ketoglutarate 2Glutamate NADPH NADP + Gln Glu

19 M2 Amino acid metabolism

20 The amino acids can be grouped into six biosynthetic families depending on the metabolic intermediate from which their carbon skeleton is derived. Biosynthesis of amino acids

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22 The 20 amino acids are synthesized mainly from intermediates of glycolysis, citric acid cycle, or pentose phosphate pathway in bacteria and plants.

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78 PEP E – 4 – P

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92 Only about half of the amino acids can be synthesized by us human being: the rest have to be obtained from diet, thus called essential amino acids.

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94 Amino Acids that can not be synthesized by human (essential Amino acids) Histidine (Arg) Isoleucine Leucine Lysine Methionine (and/or cysteine) Phenylalanine (and/or tyrosine) Threonine Tryptophan Valine

95 Amino acids are precursors of many specialized biomolecules

96 Porphyrins in mammals are made from Gly and succinyl-CoA.

97 Amino acid degradation

98 The surplus amino acids in animals can be completely oxidized or converted to othe r storable fuels Amino acids in excess can neither be stored, nor excreted, but oxidized to release energy or converted to fatty acids/glucose. Animals utilize amino acids for energy generation following a protein meal, during starvation. Microorganisms can also use amino acids as an energy source when the supply is in excess. Plants almost never use amino acids (neither fatty acids) as an energy source.

99 Dietary proteins are digested into amino acids via the action of pepsin, trypsin, chymotrypsin, carboxypeptidase and aminopeptidase

100 Aminotransferase or transaminase The -amino group of many amino acids is transferred to -ketoglutarate via catalysis of a specific aminotransferase, producing Glu and an -keto acid. This reaction is fully reversible!

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102 The major route for the deamination of amino acids is transamination followed by the oxidative deamination of glutamate. How ever, a minor route also exists that involves direct oxidation of the amino acid by L- amino acid oxidase.

103 The carbon skeletons of the amino acids are converted (funneled) into seven major metabolic intermediates before being completely oxidized via the citric acid cycle

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105 Trp, Ala, Gly, Ser, Cys are converted to pyruvate (thus being glucogenic) Part of Trp, Phe, Tyr, Leu & Lys are converted to acetoacetyl-CoA, and Part of Trp, Leu, and Ile is converted to acetyl-CoA. (thus being ketogenic)

106 Summary Atmospheric N 2 is reduced to ammonia by the dinitrogenase reductase and the dinitrogenase (containing a key Fe-Mo cofactor) of the nitrogenase complex present only in certain bacteria. Ammonia enters organic molecules via Glu and Gln. Glutamine amidotransferases catalyzes the transferring of the amide amino group to many acceptor molecules.

107 Amino acids are mainly derived from intermediates of glycolysis, the citric acid cycle, and the pentose phosphate pathway. Pro and Arg are derived from Glu, which is synthesized from -ketoglutarate. Ser, Gly, and Cys are derived from 3-phosphoglycerate. Met and Thr are derived from oxaloacetate. Lys and Ile are derived from oxaloacetate and pyruvate. Biosynthesis

108 Val and Leu are derived from pyruvate. Ile and Val are derived from Thr/pyruvate and two molecules of pyruvate respectively, using the same enzymes; Leu is derived from two molecules of pyruvate, sharing four steps of reactions with Val synthesis. Tryptophan is derived from phosphoenolpyruvate, erythrose 4-P, Gln, PRPP, and one Ser. Phe and Tyr are synthesized from two phosphoenolpyruvates, one erythrose 4-P, and one Glu.

109 Amino acid in excess can neither be stored, nor excreted, but oxidized or converted. The amino groups and carbon skeletons of amino acids take separate but interconnected pathways. Glutamate collects and delivers free ammonia. Gln and Glu releases NH 4 + in mitochondria. Degradation

110 Some amino acids are converted to intermediates of citric acid cycle by simple removal of the amino groups. Acetyl-CoA is formed from the degradation of many amino acids. A few genetic diseases are related to defects of Phe catabolism enzymes.


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