Reaction participants Show >> << Hide
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Namehelp_outline
[glutamine synthetase]-L-tyrosine
Identifier
RHEA-COMP:10660
Reactive part
help_outline
- Name help_outline L-tyrosine residue Identifier CHEBI:46858 Charge 0 Formula C9H9NO2 SMILEShelp_outline O=C(*)[C@@H](N*)CC=1C=CC(=CC1)O 2D coordinates Mol file for the small molecule Search links Involved in 18 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ATP Identifier CHEBI:30616 (Beilstein: 3581767) help_outline Charge -4 Formula C10H12N5O13P3 InChIKeyhelp_outline ZKHQWZAMYRWXGA-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,280 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
[glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine
Identifier
RHEA-COMP:10661
Reactive part
help_outline
- Name help_outline L-tyrosine-O-adenyl residue Identifier CHEBI:83624 Charge -1 Formula C19H20N6O8P SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)Oc2ccc(C[C@H](N-*)C(-*)=O)cc2)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline diphosphate Identifier CHEBI:33019 (Beilstein: 185088) help_outline Charge -3 Formula HO7P2 InChIKeyhelp_outline XPPKVPWEQAFLFU-UHFFFAOYSA-K SMILEShelp_outline OP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,129 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:18589 | RHEA:18590 | RHEA:18591 | RHEA:18592 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Mechanism of the enzymatic inactivation of glutamine synthetase from E. coli.
Wulff K., Mecke D., Holzer H.
Biochem Biophys Res Commun 28:740-745(1967) [PubMed] [EuropePMC]
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5'-adenylyl-O-tyrosine. The novel phosphodiester residue of adenylylated glutamine synthetase from Escherichia coli.
Shapiro B.M., Stadtman E.R.
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Inactivation, stabilization and some properties of ATP: glutamine synthetase adenylyltransferase from Escherichia coli B.
Wolf D., Ebner E., Hinze H.
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Reversible adenylylation of glutamine synthetase is dynamically counterbalanced during steady-state growth of Escherichia coli.
Okano H., Hwa T., Lenz P., Yan D.
Glutamine synthetase (GS) is the central enzyme for nitrogen assimilation in Escherichia coli and is subject to reversible adenylylation (inactivation) by a bifunctional GS adenylyltransferase/adenylyl-removing enzyme (ATase). In vitro, both of the opposing activities of ATase are regulated by sma ... >> More
Glutamine synthetase (GS) is the central enzyme for nitrogen assimilation in Escherichia coli and is subject to reversible adenylylation (inactivation) by a bifunctional GS adenylyltransferase/adenylyl-removing enzyme (ATase). In vitro, both of the opposing activities of ATase are regulated by small effectors, most notably glutamine and 2-oxoglutarate. In vivo, adenylyltransferase (AT) activity is critical for growth adaptation when cells are shifted from nitrogen-limiting to nitrogen-excess conditions and a rapid decrease of GS activity by adenylylation is needed. Here, we show that the adenylyl-removing (AR) activity of ATase is required to counterbalance its AT activity during steady-state growth under both nitrogen-excess and nitrogen-limiting conditions. This conclusion was established by studying AR(-)/AT(+) mutants, which surprisingly displayed steady-state growth defects in nitrogen-excess conditions due to excessive GS adenylylation. Moreover, GS was abnormally adenylylated in the AR(-) mutants even under nitrogen-limiting conditions, whereas there was little GS adenylylation in wild-type strains. Despite the importance of AR activity, we establish that AT activity is significantly regulated in vivo, mainly by the cellular glutamine concentration. There is good general agreement between quantitative estimates of AT regulation in vivo and results derived from previous in vitro studies except at very low AT activities. We propose additional mechanisms for the low AT activities in vivo. The results suggest that dynamic counterbalance by reversible covalent modification may be a general strategy for controlling the activity of enzymes such as GS, whose physiological output allows adaptation to environmental fluctuations. << Less
J Mol Biol 404:522-536(2010) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Regulation of glutamine synthetase. 8. ATP: glutamine synthetase adenylyltransferase, an enzyme that catalyzes alterations in the regulatory properties of glutamine synthetase.
Kingdon H.S., Shapiro B.M., Stadtman E.R.
Proc. Natl. Acad. Sci. U.S.A. 58:1703-1710(1967) [PubMed] [EuropePMC]
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ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties.
Ebner E., Wolf D., Gancedo C., Elsaesser S., Holzer H.