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Chapter 20 : Biosynthesis of Glutamine and Glutamate and the Assimilation of Ammonia

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Abstract:

Regulation of the enzymes involved in glutamine and glutamate biosynthesis in and their roles in ammonia assimilation is the focus of this chapter. For most bacteria, assimilation of ammonia is accomplished through the synthesis of glutamine and glutamate. Alanine dehydrogenase and asparagine synthetase have also been implicated in assimilation, and their roles are discussed. The can be separated into three groups based on the pathway used for assimilation. One group, represented by , employs glutamine synthetase (GS) and GOGAT for assimilation. The second, which contains most members of the genus, utilizes all three enzymes, depending on nutritional environment. The third group uses only GDH for assimilation, a characteristic of some N-fixing . Assimilation of ammonia in derivatives of 168 and SMY is solely accomplished through the coupled action of GS and GOGAT. A catabolic role for GDH is consistent with the notion that GOGAT is solely responsible for glutamate biosynthesis in . The production of glutamate from glutamine is accomplished by the enzyme L-glutamine aminohydrolase, also known as glutaminase.

Citation: Schreier H. 1993. Biosynthesis of Glutamine and Glutamate and the Assimilation of Ammonia, p 281-298. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch20

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Bacterial Proteins
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Amino Acids
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Nitrogen Sources
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Figures

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Figure 1

operon in (a) Structure of the operon and model for control. Autogenous control of expression from the promoter, involves and gene products GlnR and GS, respectively. GlnR represses transcription under excess-nitrogen conditions by binding to operators and , thereby inhibiting transcription initiation. GlnR activity is thought to be mediated in part by GS, which may be used to relay information about the nitrogen state of the cell, (b) Sequence of the promoter region from -71 to +5 relative to the start point of transcription ( ). Boxed sequences indicate -10 and -35 promoter regions. Diverging arrows indicate symmetrical (-40 to -60) and quasisymmetrical (-17 to -37) sites shown to be involved in GlnR binding.

Citation: Schreier H. 1993. Biosynthesis of Glutamine and Glutamate and the Assimilation of Ammonia, p 281-298. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch20
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Image of Figure 2
Figure 2

gene of The schematic diagram shows orientation of the transcript as directed from either of two promoters, and and a putative anti-g/иА transcript expressed from promoter from the opposite strand. Boxes at the beginning of each message represent regions whose sequences, shown relative to the start point of the open reading frame, are complementary to each other (see text).

Citation: Schreier H. 1993. Biosynthesis of Glutamine and Glutamate and the Assimilation of Ammonia, p 281-298. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch20
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Figure 3

and genes of . Synthesis of GOGAT large and small subunits, coded for by and respectively, are shown to occur from a monocistronic message, although such has not been established. The GltC protein, produced by represses its own synthesis and is also required for activation of transcription from the promoter under glutamate-limited growth conditions. The overlap of the two promoters and the presence of several repeated sequences within the and regions are thought to play roles in regulating transcription (see text).

Citation: Schreier H. 1993. Biosynthesis of Glutamine and Glutamate and the Assimilation of Ammonia, p 281-298. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch20
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Tables

Generic image for table
Table 1

GOGAT and GDH in gram-positive bacteria

Citation: Schreier H. 1993. Biosynthesis of Glutamine and Glutamate and the Assimilation of Ammonia, p 281-298. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch20

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