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Results 1 - 10 of 11 > >>
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EC Number Inhibitors Commentary Structure
Display the reaction diagram Show all sequences 2.7.7.892-oxoglutarate controls the extent of activation or inhibition of the enzyme by PII or PII-UMP. 2-Oxoglutarate acts exclusively through its binding to PII and PII-UMP, and does not alter the binding of PII or PII-UMP to the enzyme Go to the Ligand Summary Page
Display the reaction diagram Show all sequences 2.7.7.89AMP - Go to the Ligand Summary Page
Display the reaction diagram Show all sequences 2.7.7.89diphosphate - Go to the Ligand Summary Page
Display the reaction diagram Show all sequences 2.7.7.89glutamate - Go to the Ligand Summary Page
Display the reaction diagram Show all sequences 2.7.7.89glutamine the adenylyl-removing reaction is activated by PII-UMP and is inhibited by glutamine and by PII. PII, PII-UMP, and glutamine shift the enzyme among at least six different enzyme forms, two of which are inactive, one of which exhibits adenylyl-removing activity, and three of which exhibit adenylyltranferase activity. The PII, PII-UMP, and glutamine binding sites are in communication. Glutamine and PII-UMP compete for the enzyme Go to the Ligand Summary Page
Display the reaction diagram Show all sequences 2.7.7.89glutamine glutamine inhibition of the adenylyl-removing activity involves intramolecular signaling between the adenylyltransferase and adenylyl-removing domains Go to the Ligand Summary Page
Display the reaction diagram Show all sequences 2.7.7.89glutamine - Go to the Ligand Summary Page
Display the reaction diagram Show all sequences 2.7.7.89signal transduction protein PII the adenylyl-removing reaction is activated by PII-UMP and is inhibited by glutamine and by PII. The adenylyltransferase reaction is activated by glutamine and by the unmodified form of the PII signal transduction protein and is inhibited by the uridylylated form of PII, PII-UMP. PII, PII-UMP, and glutamine shift the enzyme among at least six different enzyme forms, two of which are inactive, one of which exhibits adenylyl-removing activity, and three of which exhibit adenylyltranferase activity. The enzyme appears to contain two distinct sites for PII and PII-UMP. The PII, PII-UMP, and glutamine sites are in communication. The binding of PII is favored by glutamine and its level reduced by PII-UMP, whereas glutamine and PII-UMP compete for the enzyme Go to the Ligand Summary Page
Display the reaction diagram Show all sequences 2.7.7.89signal transduction protein PII the deadenylylation activity of AT-N is inhibited by PII Go to the Ligand Summary Page
Display the reaction diagram Show all sequences 2.7.7.89signal transduction protein PII a tetrameric PIID molecule interacts with only one enzyme molecule at a time Go to the Ligand Summary Page
Results 1 - 10 of 11 > >>
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