نتایج جستجو برای: glutamine synthetase activity

تعداد نتایج: 1155348  

Journal: :The Journal of biological chemistry 2003
Pawel Bieganowski Helen C Pace Charles Brenner

NAD+ is an essential co-enzyme for redox reactions and is consumed in lysine deacetylation and poly(ADP-ribosyl)ation. NAD+ synthetase catalyzes the final step in NAD+ synthesis in the well characterized de novo, salvage, and import pathways. It has been long known that eukaryotic NAD+ synthetases use glutamine to amidate nicotinic acid adenine dinucleotide while many purified prokaryotic NAD+ ...

Journal: :Brain : a journal of neurology 2008
Tore Eid Arko Ghosh Yue Wang Henning Beckström Hitten P Zaveri Tih-Shih W Lee James C K Lai Gauri H Malthankar-Phatak Nihal C de Lanerolle

An excess of extracellular glutamate in the hippocampus has been linked to the generation of recurrent seizures and brain pathology in patients with medically intractable mesial temporal lobe epilepsy (MTLE). However, the mechanism which results in glutamate excess in MTLE remains unknown. We recently reported that the glutamate-metabolizing enzyme glutamine synthetase is deficient in the hippo...

Journal: :Journal of bacteriology 1967
J S Hubbard E R Stadtman

The relationships of five feedback inhibitors for the Bacillus licheniformis glutamine synthetase were investigated. The inhibitors were distinguishable by differences in their competitive relationship for the substrates of the enzyme. Mixtures of l-glutamine and adenosine-5'-monophosphate (AMP) or histidine and AMP caused synergistic inhibition of glutamine synthesis. Histidine, alanine, and g...

Journal: :Journal of general microbiology 1974
A P Sims J Toone V Box

Yeast glutamine synthetase was purified and shown to be an octameric globular protein (s = 15.4,fF0 = 1-29, mol. wt = 390000). It consists of two weakly-bound half molecules (s = 8.7, fFo = 1-35, mol. wt = 180500) and relatively harsh treatment is required to dissociate these octamers into component monomers (s = 3.8). Deactivation of the enzyme in vivo may include changes in the conformation o...

Journal: :The Journal of nutrition 2007
Yi-Fang Huang Yanxin Wang Malcolm Watford

This study examined the regulation of glutamine synthetase protein levels, in response to changes in external glutamine concentration, in mouse C2C12 skeletal muscle cells. Glutamine, at concentrations as low as 0.25 mmol/L, downregulated endogenous and exogenous (plasmid encoded) glutamine synthetase with maximal effect at 2 mmol/L. Glutamine appears to act by changing the stability of the glu...

Journal: :Journal of bacteriology 1974
S L Streicher K T Shanmugam F Ausubel C Morandi R B Goldberg

Mutations causing constitutive synthesis of glutamine synthetase (GlnC(-) phenotype) were transferred from Klebsiella aerogenes into Klebsiella pneumoniae by P1-mediated transduction. Such GlnC(-) strains of K. pneumoniae have constitutive levels of glutamine synthetase. Two of three GlnC(-) strains of K. pneumoniae studied, each containing independently isolated mutations that confer the GlnC(...

Journal: :Plant physiology 1988
P Fischer U Klein

The specific activities of nitrate reductase, nitrite reductase, glutamine synthetase, glutamate synthase, and glutamate dehydrogenase were determined in intact protoplasts and intact chloroplasts from Chlamydomonas reinhardtii. After correction for contamination, the data were used to calculate the portion of each enzyme in the algal chloroplast. The chloroplast of C. reinhardtii contained all...

Journal: :Plant physiology 1981
J H Paul K E Cooksey

The ammonium assimilatory enzymes glutamine synthetase (EC 6.3.1.2) and glutamate dehydrogenase (EC 1.4.1.3) were investigated for a possible role in the regulation of asparaginase (EC 3.5.1.1) in a Chlamydomonas species isolated from a marine environment. Cells grown under nitrogen limitation (0.1 millimolar NH(4) (+), NO(3) (-), or l-asparagine) possessed 6 times the asparaginase activity and...

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