Regulation of ammonium uptake and metabolism by nitrogen fixing bacteria. III. Clostridium pasteurianum

Kleiner, Diethelm

doi:10.1007/bf00423074

Cited by 35 publications

(15 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…GGT activity of adenylylated or NHZ-shocked E. coli GS measured in the presence of 0.3 mM-Mn2+ is unchanged after SVP treatment, whereas activity in the presence both of 0.3 mM-Mn2+ and of 60 mM-Mg2+ is greatly increased. There is no change in the GGT activity of GS from the Gram-positive bacteria Bacillus subtilis (Schreier et al, 1985), C. pasteurianum (Kleiner, 1979) and Clostridium acetobutylicurn (Usdin et al, 1986) and the archaebacterium Methanobacterium ivanovi (Bhatnagar et al, 1986) in the presence of Mn2+ or Mg2+ or Mn2+ plus Mg2+. In contrast, SVP treatment of the cloned B .…”

Section: Discussionmentioning

confidence: 99%

Novel Structure, Properties and Inactivation of Glutamine Synthetase Cloned from Bacteroides fragilis

Southern¹,

Parker²,

Woods³

1987

Microbiology

View full text Add to dashboard Cite

The cloned Bacteroides fragilis glutamine synthetase (GS) subunit produced in Escherichia coli had the same apparent M, of approximately 75000 as the GS subunit from B. fragilis cells. The B. fragilis GS enzyme had an apparent M, of approximately 490000 and it is concluded that the GS is a hexamer. The cloned GS did not appear to be regulated by adenylylation and deadenylylation and the cloned enzyme was inactivated by snake venom phosphodiesterase. The pH profiles of the cloned GS, assayed by the y-glutamyl transferase (GGT) assay were similar for NH,+-shocked and unshocked cell extracts and an isoactivity point was not obtained from these curves. The cloned GS was subject to feedback inhibition by amino acids but not by AMP. The GGT activity of the cloned GS in NH,+-shocked and unshocked cell-free extracts was inhibited by Mg2+. Mn2+ stimulated the cloned GS GGT activity of NHI-shocked cell-free extracts. Western blotting indicated that GS production was regulated by nitrogen in B. fragilis cells but cell extracts showed no GGT activity. Cloned B. fragilis GS produced in E. coli was specifically and irreversibly inactivated by B. fragilis cell extracts.

show abstract

Section: Discussionmentioning

confidence: 99%

Novel Structure, Properties and Inactivation of Glutamine Synthetase Cloned from Bacteroides fragilis

Southern¹,

Parker²,

Woods³

1987

Microbiology

View full text Add to dashboard Cite

show abstract

“…Glutamine synthetase (ATP-dependent formation of y-glutamyl hydroxamate from glutamate) and glutamate synthase were assayed according to established methods [9]. DON and MSX were from Sigma (Mi~nchen); MSF was from Riedel-De Haen (Hannover).…”

Section: Methodsmentioning

confidence: 99%

“…Klebsiella pneumoniae M5al (a gift from Professor R.H. Burris, University of Wisconsin) was grown aerobically in batches with 20 mM histidine as the nitrogen source and assayed for methylammonium uptake as in [5]. Glutamine synthetase (ATP-dependent formation of y-glutamyl hydroxamate from glutamate) and glutamate synthase were assayed according to established methods [9]. DON and MSX were from Sigma (Mi~nchen); MSF was from Riedel-De Haen (Hannover).…”

Section: Methodsmentioning

confidence: 99%

Inhibition of ammonium (methylammonium) transport in Klebsiella pneumoniae by glutamine and glutamine analogues

Kleiner

Castorph

1982

FEBS Letters

View full text Add to dashboard Cite

“…A common carrier for glutamate and aspartate was inferred from cross inhibition experiments: aspartate transport was completely inhibited by a 1000-fold 1). The smaller excretion found with N 2 can be attributed to both smaller intracellular pools [9] and slower growth: the protein content was 0.14 mg/ml and Asparagine and tryptophan could not be determined. The smaller excretion found with N 2 can be attributed to both smaller intracellular pools [9] and slower growth: the protein content was 0.14 mg/ml and Asparagine and tryptophan could not be determined.…”

Section: Clostridium Pasteurianummentioning

confidence: 80%

Uptake and excretion of amino acids by saccharolytic clostridia

Szech

Braun

Kleiner

1989

FEMS Microbiology Letters

View full text Add to dashboard Cite

Amino acid uptake and excretion in Clostridium pasteurianum, Clostridium aceticum and Clostridium butyricum were generally inversely related: in the exponential growth phase excretion of an amino acid was observed only in strains which lacked the respective amino acid carrier. C. butyricum transports all amino acids and does not show any amino acid excretion. C. aceticum takes up all amino acids but alanine, and up to 1 mM alanine is excreted. C. pasteurianum only absorbs aspartate, glutamate, glutamine, glycine and serine, hence all other amino acids (except threonine) are found in the medium. With ammonium or N2, up to 20% or 8% of the nitrogen assimilated is lost, respectively. These data emphasize the importance of transport systems in cyclic retention of metabolites.

show abstract

Regulation of ammonium uptake and metabolism by nitrogen fixing bacteria. III. Clostridium pasteurianum

Cited by 35 publications

References 25 publications

Novel Structure, Properties and Inactivation of Glutamine Synthetase Cloned from Bacteroides fragilis

Novel Structure, Properties and Inactivation of Glutamine Synthetase Cloned from Bacteroides fragilis

Inhibition of ammonium (methylammonium) transport in Klebsiella pneumoniae by glutamine and glutamine analogues

Uptake and excretion of amino acids by saccharolytic clostridia

Contact Info

Product

Resources

About