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Chapter 11 : Nitrogen Metabolism

Authors: Hilde De Reuse1, Stéphane Skouloubris1
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Affiliations: 1: Hilde De Reuse and Stephane Skouloubris • Unite de Pathogenie Bacterienne des Muqueuses Institut Pasteur, Paris, France
Content Type: Monograph
Publication Year: 2001

Category: Bacterial Pathogenesis

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Abstract:

The study of nitrogen metabolism in was initially made possible by the development of defined growth media, which permitted (i) the determination of the minimal amino acid requirements of this bacterium and (ii) the following of the fate of amino acids in whole bacteria. The subsequent publication of the complete genomic sequences of two strains, 26695 and J99, has confirmed some of the data obtained and supplied additional genetic information. is auxotrophic for several amino acids, supporting the idea that its growth in vivo is strictly dependent on the gastric environment. Large amounts of amino acids, dipeptides, and polypeptides are present in the gastric juice owing to the activities of enzymes such as pepsin, which break down proteins efficiently. Amino acid utilization by grown in a defined medium has been investigated by nuclear magnetic resonance (NMR) spectroscopy and amino acid analysis. Nitrogen metabolism in generates considerable amounts of free ammonia that either could be incorporated into proteins via the glutamine synthetase (GS-ase) pathway or released into the external environment by diffusion in its NH form. The possibility that has a urea cycle was investigated by assessing the activity of the four enzymes of this cycle: arginase, anabolic ornithine transcarbamoylase (OTC-ase), arginosuccinate synthetase, and arginosuccinase, employing one- and two-dimensional NMR spectroscopy and radioactive tracer analysis.

Citation: De Reuse H, Skouloubris S. 2001. Nitrogen Metabolism, p 125-133. In Mobley H, Mendz G, Hazell S (ed), . ASM Press, Washington, DC. doi: 10.1128/9781555818005.ch11
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Nitrogen Metabolism
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Citation: De Reuse H, Skouloubris S. 2001. Nitrogen Metabolism, p 125-133. In Mobley H, Mendz G, Hazell S (ed), . ASM Press, Washington, DC. doi: 10.1128/9781555818005.ch11
/content/10.1128/9781555818005.chap11.fig11-1
Figure 1

Nitrogen sources for The reactions are catalyzed by the following enzymes: ( ) glutaminase, ( ) L-serine deaminase, ( ) aspartate-ammonia lyase, ( ) L-asparaginase II, ( ) urease, ( ) formamidase, ( ) aliphatic amidase. The products of these deamination and deamidation reactions are also shown.

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10.1128/9781555818005/fig11-1.gif
Image of Figure 1
Figure 1

Nitrogen sources for The reactions are catalyzed by the following enzymes: ( ) glutaminase, ( ) L-serine deaminase, ( ) aspartate-ammonia lyase, ( ) L-asparaginase II, ( ) urease, ( ) formamidase, ( ) aliphatic amidase. The products of these deamination and deamidation reactions are also shown.

Citation: De Reuse H, Skouloubris S. 2001. Nitrogen Metabolism, p 125-133. In Mobley H, Mendz G, Hazell S (ed), . ASM Press, Washington, DC. doi: 10.1128/9781555818005.ch11
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Figure 2

Pathways of nitrogen assimilation in and GOGAT-ase corresponds to glutamate synthase, GDH-ase to glutamate dehydrogenase, and GS-ase to glutamine synthetase.

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10.1128/9781555818005/fig11-2.gif
Image of Figure 2
Figure 2

Pathways of nitrogen assimilation in and GOGAT-ase corresponds to glutamate synthase, GDH-ase to glutamate dehydrogenase, and GS-ase to glutamine synthetase.

Citation: De Reuse H, Skouloubris S. 2001. Nitrogen Metabolism, p 125-133. In Mobley H, Mendz G, Hazell S (ed), . ASM Press, Washington, DC. doi: 10.1128/9781555818005.ch11
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Figure 3

Enzymatic reactions of the urea cycle. Urea hydrolysis by urease in is indicated, as is the reaction producing carbamoyl phosphate.

10.1128/9781555818005/fig11-3_thmb.gif
10.1128/9781555818005/fig11-3.gif
Image of Figure 3
Figure 3

Enzymatic reactions of the urea cycle. Urea hydrolysis by urease in is indicated, as is the reaction producing carbamoyl phosphate.

Citation: De Reuse H, Skouloubris S. 2001. Nitrogen Metabolism, p 125-133. In Mobley H, Mendz G, Hazell S (ed), . ASM Press, Washington, DC. doi: 10.1128/9781555818005.ch11
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