PMID:776970: Difference between revisions
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|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=776970 PubMed] | |{{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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Revision as of 22:44, 25 April 2008
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. |
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