PMID:776970: Difference between revisions

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<span style = 'font-size: large'> '''Prusiner, S and Stadtman, ER'''  (1976) Regulation of glutaminase B in Escherichia coli. III. Control by nucleotides and divalent cations.''J. Biol. Chem.'' '''251''':3463-9</span>
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!align=left  |Citation
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'''Prusiner, S and Stadtman, ER'''  (1976) Regulation of glutaminase B in Escherichia coli. III. Control by nucleotides and divalent cations. ''J. Biol. Chem.'' '''251''':3463-9
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!align=left  |Abstract
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Glutaminase B from Escherichia coli is modulated by nucleotides and divalent cations. ATP and ADP inhibit glutaminase B whereas AMP and divalent cations activate it. Inhibition and activation required preincubation of the nucleotides with glutaminase B at 4 degrees. Mg2+, Mn2+, and Ca2+ activated the enzyme and prevented the inhibition by ATP. Dialysis in the presence of an activator ligand reversed the ATP inhibition of glutaminase B. The modulation of glutaminase B by energy charge is similar to that observed with other catabolic enzymes. We suggest that a pattern of reciprocal regulation of glutaminase B and glutamine synthetase by adenine nucleotides prevents the formation of a "futile cycle" of amide synthesis and degradation.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=776970 PubMed]


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|{{TableHeadingColor}} |'''Abstract''' || Glutaminase B from Escherichia coli is modulated by nucleotides and divalent cations. ATP and ADP inhibit glutaminase B whereas AMP and divalent cations activate it. Inhibition and activation required preincubation of the nucleotides with glutaminase B at 4 degrees. Mg2+, Mn2+, and Ca2+ activated the enzyme and prevented the inhibition by ATP. Dialysis in the presence of an activator ligand reversed the ATP inhibition of glutaminase B. The modulation of glutaminase B by energy charge is similar to that observed with other catabolic enzymes. We suggest that a pattern of reciprocal regulation of glutaminase B and glutamine synthetase by adenine nucleotides prevents the formation of a "futile cycle" of amide synthesis and degradation.
!align=left  |Keywords
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Calcium/pharmacology; Energy Transfer; Enzyme Activation/drug effects; Escherichia coli/enzymology; Glutaminase/metabolism; Kinetics; Magnesium/pharmacology; Manganese/pharmacology; Osmolar Concentration; Potassium Chloride/pharmacology; Ribonucleotides/pharmacology; Sodium Chloride/pharmacology; Temperature
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=776970 PubMed]
 
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Latest revision as of 04:51, 15 September 2013

Citation

Prusiner, S and Stadtman, ER (1976) Regulation of glutaminase B in Escherichia coli. III. Control by nucleotides and divalent cations. J. Biol. Chem. 251:3463-9

Abstract

Glutaminase B from Escherichia coli is modulated by nucleotides and divalent cations. ATP and ADP inhibit glutaminase B whereas AMP and divalent cations activate it. Inhibition and activation required preincubation of the nucleotides with glutaminase B at 4 degrees. Mg2+, Mn2+, and Ca2+ activated the enzyme and prevented the inhibition by ATP. Dialysis in the presence of an activator ligand reversed the ATP inhibition of glutaminase B. The modulation of glutaminase B by energy charge is similar to that observed with other catabolic enzymes. We suggest that a pattern of reciprocal regulation of glutaminase B and glutamine synthetase by adenine nucleotides prevents the formation of a "futile cycle" of amide synthesis and degradation.

Links

PubMed

Keywords

Calcium/pharmacology; Energy Transfer; Enzyme Activation/drug effects; Escherichia coli/enzymology; Glutaminase/metabolism; Kinetics; Magnesium/pharmacology; Manganese/pharmacology; Osmolar Concentration; Potassium Chloride/pharmacology; Ribonucleotides/pharmacology; Sodium Chloride/pharmacology; Temperature

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