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

Author: Harold J. Schreier1
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Affiliations: 1: Center of Marine Biotechnology, University of Maryland, 600 East Lombard Street, Baltimore, Maryland 21202, and Department of Biological Sciences, University of Maryland Baltimore County, Baltimore, Maryland 21228
Content Type: Monograph
Publication Year: 1993

Category: Bacterial Pathogenesis; Microbial Genetics and Molecular Biology

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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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Biosynthesis of Glutamine and Glutamate and the Assimilation of Ammonia
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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
/content/10.1128/9781555818388.chap20.fig20-1
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.

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10.1128/9781555818388/fig20-1.gif
Image of Figure 1
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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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).

10.1128/9781555818388/fig20-2_thmb.gif
10.1128/9781555818388/fig20-2.gif
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).

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10.1128/9781555818388/fig20-3.gif
Image of Figure 3
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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References

/content/book/10.1128/9781555818388.chap20
1. Aharonowitz, Y.,, and C. G. Friedrich. 1980. Alanine dehydrogenase of the j3-lactam producer Streptomyces clavuligerus. Arch. Microbiol. 125: 137– 142.
2. Albertini, A. M.,, and A. Galizzi. 1990. The Bacillus subtilis outB gene is highly homologous to an Esche-richia coli nir-like gene. J. Bacteriol. 172: 5482– 5485.
3. Aronson, J. N. 1975. Ammonia assimilation and glutamate catabolism by Bacillus thuringiensis. Microbiology 1975: 444– 449.
4. Atkinson, M. R.,, and S. H. Fisher. 1991. Identification of genes and gene products whose expression is activated during nitrogen-limited growth in Bacillus subtilis. J. Bacteriol. 173: 23– 27.
5. Behrmann, I.,, D. Hillemann,, A. Puhler,, E. Strauch,, and W. Wohlleben. 1990. Overexpression of a Streptomyces viridochromogenes gene (glnll) encoding glutamine synthetase similar to those of eucaryotes confers resistance against the antibiotic phosphoinothricyl-alanyl-ala-nine. J. Bacteriol. 172: 5326– 5334.
6. Bender, R. A. 1991. The role of the Nac protein in the nitrogen regulation of Klebsiella aerogenes. Mol. Microbiol. 5: 2575– 2580.
7. Berberich, R.,, M. Kaback,, and E. Freese. 1968. D-Amino acids as inducers of L-alanine dehydrogenase in Bacillus subtilis. J. Biol. Chem. 243: 1006– 1011.
8. Bernlohr, R. W. 1967. Changes in amino acid permeation during sporulation. J. Bacteriol. 93: 1031– 1044.
9. Bernlohr, R. W.,, H. J. Schreier,, and T. J. Donohue. 1984. Enzymes of glutamate and glutamine biosynthesis in Bacillus licheniformis. Curr. Top. Cell. Regul. 24: 145– 152.
10. Bohannon, D. E.,, M. S. Rosenkrantz,, and A. L. Sonenshein. 1985. Regulation of Bacillus subtilis glutamate synthase genes by the nitrogen source. J. Bacteriol. 163: 957– 964.
11. Bohannon, D. E.,, H. J. Schreier,, and A. L. Sonenshein. Unpublished data.
12. Bohannon, D. E.,, and A. L. Sonenshein. 1989. Positive regulation of glutamate biosynthesis in Bacillus subtilis. J. Bacteriol. 171: 4718– 4727.
13. Bohannon, D. E.,, and A. L. Sonenshein,. 1990. GltC, the positive regulator of glutamate synthase gene expression, p. 141– 145. In J. A. Hoch, and A. T. Ganesan (ed.), Genetics and Biotechnology of Bacilli. Academic Press, Inc., New York.
14. Bott, K. F.,, G. Reysset,, J. Grégoire,, D. Islert,, and J.-P. Aubert. 1977. Characterization of glutamine requiring mutants of Bacillus subtilis. Biochem. Biophys. Res. Commun. 79: 996– 1003.
15. Bower, S.,, and H. Zalkin. 1983. Chemical modification and ligand binding studies with Escherichia coli glutamate synthase. Biochemistry 22: 1613– 1620.
16. Brana, A. F.,, N. Paiva,, and A. L. Demain. 1986. Pathways and regulation of ammonium assimilation in Streptomyces clavuligerus. J. Gen. Microbiol. 132: 1305– 1317.
17. Brown, S. B.,, and A. L. Sonenshein. Submitted for publication.
18. Buono, F.,, R. Testa,, and D. G. Lundgren. 1966. Physiology of growth and sporulation in Bacillus cereus. I. Effect of glutamic and other amino acids. J. Bacteriol. 91: 2291– 2299.
19. Burchall, J. J.,, E. C. Reichelt,, and M. J. Wolin. 1964. Purification and properties of the asparagine synthetase of Streptococcus bovis. J. Biol. Chem. 239: 1794– 1798.
20. Charba, J. F.,, and H. M. Nakata. 1977. Role of glutamate in the sporogenesis of Bacillus cereus. J. Bacteriol. 130: 242– 248.
21. Charney, J.,, W. P. Fisher,, and C. P. Hegarty. 1951. Manganese as an essential element for sporulation in the genus Bacillus. J. Bacteriol. 62: 145– 148.
22. Clark, V. L.,, D. E. Peterson,, and R. W. Bernlohr. 1972. Changes in free amino acid production and intracellu-lar amino acid pools of Bacillus licheniformis as a function of culture age and growth media. J. Bacteriol. 112: 715– 725.
23. Cook, W. H.,, J. H. Hoffman,, and R. W. Bernlohr. 1981. Occurrence of an inducible glutaminase in Bacillus licheniformis. J. Bacteriol. 148: 365– 367.
24. Dainty, R. H. 1972. Glutamate biosynthesis in Clostrid-ium pasteurianum and its significance in nitrogen metabolism. Biochem. J. 126: 1055– 1056.
25. Dean, D. R.,, and A. I. Aronson. 1980. Selection of Bacillus subtilis mutants impaired in ammonia assimilation. J Bacteriol. 141: 985– 988.
26. Dean, D. R.,, J. A. Hoch,, and A. I. Aronson. 1977. Alteration of the Bacillus subtilis glutamine synthetase results in overproduction of the enzyme. J. Bacteriol. 131: 981– 987.
27. Débarbouille, M.,, I. Martin-Verstraete,, F. Kunst,, and G. Rapoport. 1991. The Bacillus subtilis sigL gene encodes an equivalent of o 34 from gram-negative bacteria. Proc. Natl. Acad. Sci. USA 88: 9092– 9096.
28. Deshpande, K. L.,, J. R. Katze,, and J. F. Kane. 1980. Regulation of glutamate synthase from Bacillus subtilis by glutamine. Biochem. Biophys. Res. Commun. 95: 55– 60.
29. Deshpande, K. L.,, J. R. Katze,, and J. F. Kane. 1981. Effect of glutamine on enzymes of nitrogen metabolism in Bacillus subtilis. J. Bacteriol. 145: 768– 774.
30. Deuel, T.,, and E. R. Stadtman. 1970. Some kinetic properties of Bacillus subtilis glutamine synthetase. J. Biol. Chem. 245: 5206– 5213.
31. Deuel, T. F. 1971. Bacillus subtilis glutamine synthetase. Specific catalytic changes associated with limited sulfhydryl modification. J. Biol. Chem. 246: 599– 605.
32. Deuel, T. F.,, A. Ginsberg,, J. Yeh,, E. Shelton,, and E. R. Stadtman. 1970. Bacillus subtilis glutamine synthetase. J. Biol. Chem. 245: 5195– 5205.
33. Deuel, T. F.,, and S. Prusiner. 1974. Regulation of glutamine synthetase from Bacillus subtilis by divalent cations, feedback inhibitors and L-glutamine. J. Biol. Chem. 249: 257– 264.
34. Donohue, T. J.,, and R. W. Bemlohr,. 1978. Carbon and nitrogen catabolite repression, metabolite pools, and the regulation of sporulation in Bacillus licheniformis, p. 293– 298. In G. Chambliss, and J. C. Vary (ed.), Spores VII. American Society for Microbiology, Washington, D.C.
35. Donohue, T. J.,, and R. W. Bemlohr. 1978. Effect of cultural conditions on the concentrations of metabolic intermediates during growth and sporulation of Bacillus licheniformis. J. Bacteriol. 135: 363– 372.
36. Donohue, T. J.,, and R. W. Bemlohr. 1981. Properties of the Bacillus licheniformis A5 glutamine synthetase purified from cells grown in the presence of ammonia or nitrate. J. Bacteriol. 147: 589– 601.
37. Donohue, T. J.,, and R. W. Bemlohr. 1981. Regulation of the activity of the Bacillus licheniformis A5 glutamine synthetase. J. Bacteriol. 148: 174– 182.
38. Elmerlch, C. 1972. Le cycle du glutamate, point de depart du metabolisme de l'azote, chez Bacillus mega-terium. Eur. J. Biochem. 27: 216– 224.
39. Elmerlch, C.,, and J. Aubert. 1972. Role of glutamine synthetase in the repression of bacterial sporulation. Biochem. Biophys. Res. Commun. 46: 892– 897.
40. Elmerlch, C.,, and J.-P. Aubert. 1971. Synthesis of glutamate by a glutamine: 2-oxo-glutarate amidotrans-ferase (NADP oxidoreductase) in Bacillus megaterium. Biochem. Biophys. Res. Commun. 42: 371– 376.
41. Elmerlch, C.,, and J.-P. Aubert,. 1975. Involvement of glutamine synthetase and the purine nucleotide pathway in repression of bacterial sporulation, p. 385– 390. In P. Gerhardt,, R. N. Costilow,, and H. L. Sadoff (ed.), Spores VI. American Society for Microbiology, Washington, D.C.
42. Epstein, I.,, and N. Grossowicz. 1975. Purification and properties of glutamate dehydrogenase from a thermo-philic Bacillus. J. Bacteriol. 122: 1257– 1264.
43. Fisher, S. H. 1989. Glutamate synthesis in Streptomyces coelicolor. J. Bacteriol. 171: 2372– 2377.
44. Fisher, S. H.,, M. S. Rosenkrantz,, and A. L. Sonensheln. 1984. Glutamine synthetase gene of Bacillus subtilis. Gene 32: 427– 438.
45. Fisher, S. H.,, and A. L. Sonensheln. 1977. Glutamine requiring mutants of Bacillus subtilis. Biochem. Biophys. Res. Commun. 79: 987– 996.
46. Fisher, S. H.,, and A. L. Sonensheln. 1984. Bacillus subtilis glutamine synthetase mutants pleiotropically altered in glucose catabolite repression. J. Bacteriol. 157: 612– 621.
47. Fisher, S. H.,, and A. L. Sonensheln. 1991. Control of carbon and nitrogen metabolism in Bacillus subtilis. Annu. Rev. Microbiol. 45: 107– 135.
48. Fisher, S. H.,, and J. L. V. Wray. 1989. Regulation of glutamine synthetase in Streptomyces coelicolor. J. Bacteriol. 171: 2378– 2383.
49. Freese, E.,, S. W. Park,, and M. Cashel. 1964. The developmental significance of alanine dehydrogenase in Bacillus subtilis. Proc. Natl. Acad. Sci. USA 51: 1164– 1172.
50. Gardner, A. L.,, and A. I. Aronson. 1984. Expression of the Bacillus subtilis gene for glutamine synthetase in Escherichia coli. J. Bacteriol. 158: 967– 971.
51. Grafe, U.,, H. Boeker,, and H. Thrum. 1977. Regulative influence of o-aminobenzoic acid on the biosynthesis of nourseothricin in cultures of Streptomyces noursei JA3890b. II. Regulation of glutamine synthetase and the role of the glutamine synthetase/glutamate syn-thase pathway. Z. Allg. Mikrobiol. 17: 201– 209.
52. Grimshaw, C. E.,, and W. W. Cleland. 1981. Kinetic mechanism of Bacillus subtiUs L-alanine dehydrogenase. Biochemistry 20: 5650– 5655.
53. Gutowski, J. C.,, and H. J. Schreier. 1992. Interaction of the Bacillus subtilis glnRA repressor with operator and promoter regions in vivo. J. Bacteriol. 174: 671– 681.
54. Hemmila, I. A.,, and P. I. Mantsala. 1978. Purification and properties of glutamate synthase and glutamate dehydrogenase from Bacillus megaterium. B iochem. J. 173: 45– 52.
55. Hill, R. T.,, J. R. Parker,, H. J. K. Goodman,, D. T. Jones,, and D. R. Woods. 1988. Molecular analysis of a novel glutamine synthetase of the anaerobe Bacteroides fragi-lis.J . Gen. Microbiol. 135: 3271– 3279.
56. Hsu, R.,, S. J. Singer,, P. Keim,, T. F. Deuel,, and R. L. Heinrlkson. 1977. Structural studies of Bacillus subtilis glutamine synthetase. Further purification, sulfhydryl groups, and the NH 2-terminal amino acid sequence. Arch. Biochem. Biophys. 178: 644– 651.
57. Hubbard, J. S.,, and E. R. Stadtman. 1967. Regulation of glutamine synthetase. II. Patterns of feedback inhibition in microorganisms. J. Biol. Chem. 93: 1045– 1055.
58. Hubbard, J. S.,, and E. R. Stadtman. 1967. Regulation of glutamine synthetase. V. Partial purification and properties of glutamine synthetase from Bacillus licheniformis. J. Bacteriol. 94: 1007– 1015.
59. Janssen, P.,, and A. L. Sonensheln. Personal communication.
60. Janssen, P. J.,, W. A. Jones,, D. T. Jones,, and D. R. Woods. 1988. Molecular analysis and regulation of the glnA gene of the gram-positive anaerobe Clostridium acetobutylicum. J. Bacteriol. 170: 400– 408.
61. Kanamori, K.,, R. L. Weiss,, and J. D. Roberts. 1987. Ammonia assimilation in Bacillus polymyxa. 15N NMR and enzymatic studies. J. Biol. Chem. 262: 11038– 11045.
62. Kanamori, K.,, R. L. Weiss,, and J. D. Roberts. 1987. Role of glutamate dehydrogenase in ammonia assimilation in nitrogen-fixing Bacillus macérons. J. Bacteriol. 169: 4692– 1695.
63. Kanamori, K.,, R. L. Weiss,, and J. D. Roberts. 1989. Ammonia assimilation pathways in nitrogen-fixing Clostridium kluyverii and Clostridium butyricum. J. Bacteriol. 171: 2148– 2154.
64. Kane, J. F.,, and K. L. Deshpande. 1979. Properties of glutamate dehydrogenase from Bacillus subtilis. Biochem. Biophys. Res. Commun. 88: 761– 767.
65. Kane, J. F.,, J. Waklm,, and R. S. Fischer. 1981. Regulation of glutamate dehydrogenase in Bacillus subtilis. J. Bacteriol. 148: 1002– 1005.
66. Kun, C.-H.,, and T. C. Hollocher. 1982. I3N isotope studies on the pathway of ammonia assimilation in Bacillus megaterium and Escherichia coli. J . Bacteriol. 151: 358– 366.
67. Klmura, K.,, A. Miyakawa,, T. Imai,, and T. Sadakawa. 1977. Glutamate dehydrogenase from Bacillus subtilis PCI 219. J. Biochem. 81: 467– 476.
68. Kleiner, D. 1979. Regulation of ammonium uptake and metabolism by nitrogen fixing bacteria. III. Clostridium pasteurianum. Arch. Microbiol. 120: 263– 270.
69. Krlshnan, I. S.,, R. K. Slnghal,, and R. D. Dua. 1986. Purification and characterization of glutamine synthetase from Clostridium pasteurianum. Biochemistry 25: 1589– 1599.
70. Kumada, Y.,, E. Takano,, K. Nagaoka, and C. J. Thompson. 1990. Streptomyces hygroscopicus has two glutamine synthetase genes. J. Bacteriol. 172: 5343– 5351.
71. Leonard, C. G.,, R. D. Housewright,, and C. B. Thorne. 1962. Effects of metal ions on the optical specificity of glutamine synthetase and glutamyl transferase of Bacillus licheniformis. Biochim. Biophys. Ada 62: 432– 434.
72. Madonna, M. J.,, R. L. Fuchs,, and J. E. Brenchley. 1985. Fine-structure analysis of Salmonella typhimurium glutamate synthase genes. J. Bacteriol. 161: 353– 360.
73. Magasanik, B. 1982. Genetic control of nitrogen assimilation in bacteria. Annu. Rev. Genet. 16: 135– 168.
74. Magasanik, B. 1988. Reversible phosphorylation of an enhancer binding protein regulates the transcription of bacterial nitrogen utilization genes. Trends Biochem. Sci. 13: 475– 479.
75. Magasanik, B.,, and F. C. Neidhardt,. 1987. Regulation of carbon and nitrogen utilization, p. 1321– 1325. In F. C. Neidhardt,, J. L. Ingraham,, K. B. Low,, B. Magasanik,, M. Schaechter,, and H. E. Umbarger (ed.), Esch-erichia coli and Salmonella tyhimurium: Cellular and Molecular Biology, vol. 2. American Society for Microbiology, Washington, D.C.
76. Matsuoka, K.,, and K. Klmura. 1986. Glutamate syn-thase from Bacillus subtilis PCI 219. J. Biochem. 99: 1087– 1100.
77. McCowen, S. M.,, and P. V. Phibbs, Jr. 1974. Regulation of alanine dehydrogenase in Bacillus licheniformis. J. Bacteriol. 118: 590– 597.
78. Meers, J. L.,, and L. K. Pedersen. 1972. Nitrogen assimilation by Bacillus licheniformis organisms growing in chemostat cultures. J. Gen. Microbiol. 70: 277– 286.
79. Meers, J. L.,, D. W. Tempest,, and C. M. Brown. 1970. 'Glutamine(arnide):2-oxoglutarate amino transferase oxido-reductase (NADP)', an enzyme involved in the synthesis of glutamate by some bacteria. J. Gen. Microbiol. 64: 187– 194.
80. Nakano, Y.,, K. Chiaki,, E. Tanaka,, K. Kimura,, and K. Horikoshi. 1989. Nucleotide sequence of the glutamine synthetase gene (glnA) and its upstream region from Bacillus cereus. J. Biochem. 106: 209– 215.
81. Nakano, Y.,, M. Itoh,, E. Tanaka, and K. Kimura. 1990. Identification of the reactive cysteinyl residue and ATP binding site in Bacillus cereus glutamine synthetase by chemical modification. J. Biochem. 107: 180– 183.
82. Nakano, Y.,, and K. Kimura. 1987. Independent bindings of Mn 2+ and Mg 2+ to the active site of B. cereus glutamine synthetase. Biochem. Biophys. Res. Commun. 142: 475– 482.
83. Nakano, Y.,, and K. Kimura. 1991. Purification and characterization of a repressor for the Bacillus cereus glnRA operon. J. Biochem. 109: 223– 228.
84. Nakano, Y.,, E. Tanaka,, C. Kato,, K. Kimura,, and K. Horikoshi. 1989. The complete nucleotide sequence of the glutamine synthetase gene (glnA) of Bacillus subtilis. FEMS Microbiol. Lett. 57: 81– 86.
85. Nomellini, J. F.,, and H. J. Schreier. Unpublished data.
86. Ohshima, T.,, and K. Soda. 1979. Purification and properties of alanine dehydrogenase from Bacillus sphaeri-cus. Eur. J. Biochem. 100: 29– 39.
87. Oliver, G.,, G. Gosset,, R. Sanchez-Pescador,, E. Loyoza,, L. M. Ku,, N. Flores, B. Becerril, F. Valle, and F. Bolivar. 1987. Determination of the nucleotide sequence for the glutamate synthase structural genes of Escherichia coli K-12. Gene 60: 1– 11.
88. Opheim, D. J.,, and R. W. Bernlohr. 1975. Purification and regulation of fructose-1,6-bisphosphatase from Bacillus licheniformis. J. Biol. Chem. 250: 3024– 3033.
89. Pan, F. L.,, and J. G. Coote. 1979. Glutamine synthetase and glutamate synthase activities during growth and sporulation of Bacillus subtilis. J. Gen. Microbiol. 112: 373– 377.
90. Paress, P. S.,, and S. L. Stretcher. 1985. Glutamine synthetase of Streptomyces cattleya: purification and regulation of synthesis. J. Gen. Microbiol. 131: 1903– 1910.
91. Phibbs, P. V., Jr.,, and R. W. Bernlohr. 1971. Purification, properties and regulation of glutamic dehydrogenase of Bacillus licheniformis. J. Bacteriol. 106: 375– 385.
92. Prusiner, S., 1973. Glutaminases of Escherichia coli: properties, regulation and evolution, p. 293– 316. In S. Prusiner, and E. R. Stadtman (ed.), The Enzymes of Glutamine Metabolism. Academic Press, Inc., New York.
93. Ramaley, R. F.,, N. Fernald,, and T. De Vries. 1972. Dicarboxylate ω-amidase of Bacillus subtilis-16S: evidence for a membrane-associated form. Arch. Biochem. Biophys. 153: 88– 94.
94. Ravel, J. M. 1970. Asparagine synthetase (Lactobacillus arabinosus). Methods Enzymol. 17(A): 722– 726.
95. Rebelle, J. L.,, and N. Strauss. 1969. Regulation of glutamine synthase in Bacillus subtilis. J. Bacteriol. 148: 653– 658.
96. Reitzer, L. J.,, and B. Magasanik,. 1987. Ammonia assimilation and the biosynthesis of glutamine, glutamate, aspartate, asparagine, L-alanine, and D-alanine, p. 302– 320. In F. C. Neidhardt,, J. L. Ingraham,, K. B. Low,, B. Magasanik,, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella tyhimurium: Cellular and Molecular Biology, vol. 1. American Society for Microbiology, Washington, D.C.
97. Reysset, G. 1981. New class of Bacillus subtilis glu-tamine-requiring mutants. J. Bacteriol. 148: 653– 658.
98. Rochefort, D. A.,, and D. R. Benson. 1990. Molecular cloning, sequencing, and expression of the glutamine synthetase II iglnll) gene from the actinomycete root nodule symbiont Frankia sp. strain Cpll. J. Bacteriol. 172: 5335– 5342.
99. Ryu, J.-I. 1978. Pleiotropic effect of a rifampicin-resis-tant mutation in Bacillus subtilis. J. Bacteriol. 135: 408– 414.
100. Ryu, J.-I. 1979. Ribonucleic acid polymerase mutation affecting glutamate synthase activity in and sporulation of Bacillus subtilis. J. Bacteriol. 139: 652– 656.
101. Schaeffer, P.,, J. Millet,, and J.-P. Aubert. 1965. Cata-bolic repression of bacterial sporulation. Proc. Nail. Acad.Sci. USA 54: 704– 711.
102. Schmidt, C. N. G.,, and L. Jervis. 1982. Partial purification and characterization of glutamate synthase from a thermophilic bacillus. J. Gen. Microbiol. 128: 1713– 1718.
103. Schreier, H. J. Unpublished data.
104. Schreier, H. J.,, and R. W. Bernlohr. 1984. Purification and properties of glutamate synthase from Bacillus UcheniformL . J. Bacteriol. 160: 591– 599.
105. Schreier, H. J.,, S. W. Brown,, K. D. Hirschi,, J. F. Nomellini,, and A. L. Sonenshein. 1989. Regulation of Bacillus subtilis glutamine synthetase gene expression by the product of the glnR gene. J. Mol. Biol. 210: 51– 63.
106. Schreier, H. J.,, S. H. Fisher,, and A. L. Sonenshein. 1985. Regulation of expression from the glnA promoter of Bacillus subtilis requires the glnA gene product. Proc. Natl. Acad. Set. USA 82: 3375– 3379.
107. Schreier, H. J.,, K. D. Hirschi,, and C. A. Rostkowskl,. 1990. cts-acting sequences regulating glnRA expression in Bacillus subtilis, p. 81– 87. In J. A. Hoch, and A. T. Ganesan (ed.), Genetics and Biotechnology of Bacilli. Academic Press, Inc., New York.
108. Schreier, H. J.,, and C. A. Rostkowskl. Unpublished data.
109. Schreier, H. J.,, C. A. Rostkowskl,, and E. M. Kellner. 1993. Altered regulation of the glnRA operon in a Bacillus subtilis mutant that produces methionine sul-foximine-tolerant glutamine synthetase. J. Bacteriol. 175: 892– 897.
110. Schreier, H. J.,, C. A. Rostkowskl,, J. F. Nomellini,, and K. D. Hirschi. 1991. Identification of DNA sequences involved in regulating Bacillus subtilis glnRA expression by the nitrogen source. J. Mol. Biol. 220: 241– 253.
111. Schreier, H. J.,, T. M. Smith,, and R. W. Bernlohr. 1982. Regulation of nitrogen catabolic enzymes in Bacillus spp. J. Bacteriol. 151: 971– 975.
112. Schreier, H. J.,, T. M. Smith,, T. J. Donohue,, and R. W. Bernlohr,. 1981. Regulation of nitrogen metabolism and sporulation in Bacillus licheniformis, p. 138– 141. In H. Levinson,, A. L. Sonenshein,, and D. J. Tipper (ed.), Sporulation and Germination. American Society for Microbiology, Washington, D.C.
113. Schreier, H. J.,, and A. L. Sonenshein. 1986. Altered regulation of the glnA gene in glutamine synthetase mutants of Bacillus subtilis. J. Bacteriol. 167: 35– 43.
114. Shapiro, S.,, and L. C. Vining. 1983. Nitrogen metabolism and chloramphenicol production in Streptomyces venezuelae. Can. J. Microbiol. 29: 1706– 1714.
115. Smith, I., 1989. Initiation of sporulation, p. 185– 210. In I. Smith,, R. Slepecky,, and P. Setlow (ed.), Regulation of Prokaryotic Development. American Society for Microbiology, Washington, D.C.
116. Strauch, M. A.,, A. I. Aronson,, S. W. Brown,, H. J. Schreier,, and A. L. Sonenshein. 1988. Sequence of the Bacillus subtilis glutamine synthetase gene region. Gene 71: 257– 265.
117. Streicher, S.,, and B. Tyler. 1981. Regulation of glutamine synthetase activity by adenylylation in the gram-positive bacterium Streptomyces cattleya. Proc. Natl. Acad. Sci. USA 78: 229– 233.
118. Switzer, R. L.,, M. R. Maurizi,, J. Y. Wong,, and K. L. Flom,. 1979. Selective inactivation and degradation of enzymes in sporulating bacteria, p. 65– 79. In D. E. Atkinson, and C. F. Fox (ed.), Modulation of Protein Function. Academic Press, Inc., New York.
119. Tempest, D. W.,, J. L. Meers,, and C. M. Brown. 1970. Influence of environment on the content and composition of microbial free amino acid pools. J. Gen. Microbiol. 64: 174– 185.
120. Tyler, B. 1978. Regulation of the assimilation of nitrogen compounds. Annu. Rev. Biochem. 47: 1127– 1162.
121. Usdin, K. P.,, H. Zappe,, D. T. Jones,, and D. R. Woods. 1986. Cloning, expression and purification of glutamine synthetase from Clostridium acetobutylicum. Appl. Environ. Microbiol. 52: 413– 419.
122. Vancurova, I.,, A. Vancura,, J. Vole,, J. Kopecky,, J. Neuzil,, G. Basarova,, and V. Behal. 1989. Purification and properties of NADP-dependent glutamate dehydro-genase from Streptomyces fradiae. J. Gen. Microbiol. 135: 3311– 3318.
123. Vasantha, N.,, and E. Freese. 1979. The role of manganese in growth and sporulation of Bacillus subtilis. J. Gen. Microbiol. 112: 329– 336.
124. Wedler, F. C.,, J. Carfi,, and A. E. Ashour. 1976. Glutamine synthetase of Bacillus stearothermophilus. Regulation, site interactions, and functional information. Biochemistry 15: 1749– 1755.
125. Wedler, F. C.,, R. M. Kenney,, A. E. Ashour,, and J. Carfi. 1978. Two regulatory isozymes of glutamine synthetase from Bacillus caldolyticus, an extreme thermophile. Biochem. Biophys. Res. Commun. 81: 122– 126.
126. Wedler, F. C.,, D. S. Shreve,, K. E. Fisher,, and D. J. Merkler. 1981. Complementarity of regulation for the two glutamine synthetases from Bacillus caldolyticus, an extreme thermophile. Arch. Biochem. Biophys. 211: 276– 287.
127. Wedler, F. C.,, D. S. Shreve,, R. M. Kenney,, A. E. Ashour,, J. Carfi,, and S. G. Rhee. 1980. Two glutamine synthetases from Bacillus caldolyticus, an extreme thermophile. J. Biol. Chem. 255: 9507– 9516.
128. Wiame, J.-M.,, M. Grenson,, and H. N. Arst, Jr. 1985. Nitrogen catabolite repression in yeasts and filamentous fungi. Adv. Microb. Physiol. 26: 1– 88.
129. Winnacker, E. L.,, and H. A. Barker. 1970. Purification and properties of a NAD-dependent glutamate dehydro-genase from Clostridium SB 4. Biochim. Biophys. Acta 212: 225– 242.
130. Woods, D. R. Personal communication.
131. Wray, L. V., Jr.,, M. R. Atkinson,, and S. H. Fisher. 1991. Identification and cloning of the glnR locus, which is required for transcription of the glnA gene in Streptomyces coelicolor A3(2). J. Bacteriol. 173: 7351– 7360.
132. Wray, L. V., Jr.,, and S. H. Fisher. 1988. Cloning and nucleotide sequence of the Streptomyces coelicolor gene encoding glutamine synthetase. Gene 71: 247– 256.
133. Yoshida, A.,, and E. Freese. 1965. Enzymatic properties of alanine dehydrogenase of Bacillus subtilis. Biochim. Biophys. Acta 96: 248– 262.
134. Zhang, J.,, M. Strauch,, and A. I. Aronson. 1989. Glutamine auxotrophs of Bacillus subtilis that overproduce glutamine synthetase antigen have altered conserved amino acids in or near the active site. J. Bacteriol. 171: 3572– 3574.

Tables

Biosynthesis of Glutamine and Glutamate and the Assimilation of Ammonia
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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
/content/10.1128/9781555818388.chap20.tab20-1
Table 1

GOGAT and GDH in gram-positive bacteria

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10.1128/9781555818388/tab20-1.gif
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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