2.7.7.42: [glutamine synthetase] adenylyltransferase
This is an abbreviated version!
For detailed information about [glutamine synthetase] adenylyltransferase, go to the full flat file.
Word Map on EC 2.7.7.42
Reaction
Synonyms
adenosine triphosphate:glutamine synthetase adenylyltransferase, adenylyltransferase, adenylyltransferase, glutamine synthetase, ATASE, ATP:glutamine synthetase adenylyltransferase, ATP:[L-glutamate:ammonia ligase (ADP-forming)] adenylyl transferase, GlnE, glutamine synthetase adenylyl transferase, glutamine synthetase adenylyltransferase, glutamine synthetase ATase, glutamine-synthetase adenylyltransferase, GS ATase, [glutamate-ammonia-ligase] adenylyltransferase
ECTree
2.7.7.42 [glutamine synthetase] adenylyltransferaseAdvanced search results
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results (Activating Compound
Activating Compound on EC 2.7.7.42 - [glutamine synthetase] adenylyltransferase
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
2-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
PII proteins
-
PII proteins only stimulate the adenylylation activity of ATase
-
signal transduction protein PII-UMP
-
activates the adenylyl-removing reaction, enzyme appears to have two distinct sites for signal transduction protein PII and signal transduction protein PII-UMP
alpha-ketoglutarate
-
regulates both adenylyltransferase and adenylyl-removing reaction, acts through its binding to signal transduction protein PII and signal transduction protein PII-UMP does not alter the binding of signal transduction protein PII or signal transduction protein PII-UMP to the enzyme, adenylyltransferase assay with 0.05 mM and adenylyl-removing assay with 1 mM alpha-ketoglutarate
Gln
-
C-terminal truncation constructs are dependent on Gln for full adenylylation activity
Gln
-
wild-tpye AT needs both signal transduction protein PII and Gln to stimulate full adenylylation activity
glutamine
-
binding of PII signal transduction to ATase is stimulated by glutamine
glutamine
-
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 PII, PII-UMP, and glutamine binding sites are in communication. Glutamine and PII-UMP compete for the enzyme
L-glutamine
-
in presence of saturating amounts of PIIA protein Mg2+-supported activity is activated, Mn2+-supported activity is almost unchanged
L-glutamine
-
establishes feed-back control by stimulating the adenylylation and inactivation of the [L-glutamate:ammonia ligase (ADP-forming)]
L-glutamine
-
adenylyltransferase reaction is activated by glutamine, enzyme contains one site for glutamine, sites of signal transduction protein PII, signal transduction protein PII-UMP and glutamine are in communication, glutamine favours binding of signal transduction protein PII but competes with signal transduction protein PII-UMP for the enzyme
PII regulatory protein
-
3-5fold stimulation without glutamine, pH-independent in the range of pH 7.2-8.5
PII regulatory protein
-
activity is modulated by a regulatory protein PII, which exists in two interconvertible forms, PIIA and PIID, the unmodified form PIIA stimulates the adenylylation of [L-glutamate:ammonia ligase (ADP-forming)] , the uridylated form PIID is required for deadenylylation
PII regulatory protein
-
activity is modulated by a regulatory protein PII, which exists in two interconvertible forms, PIIA and PIID, the unmodified form PIIA stimulates the adenylylation of [L-glutamate:ammonia ligase (ADP-forming)] , the uridylated form PIID is required for deadenylylation
PII regulatory protein
-
PIIA is required
PII regulatory protein
-
activity is modulated by a regulatory protein PII, which exists in two interconvertible forms, PIIA and PIID, the unmodified form PIIA stimulates the adenylylation of [L-glutamate:ammonia ligase (ADP-forming)] , the uridylated form PIID is required for deadenylylation
PII signal transduction protein
-
0.0004 mM, activates the adenylyltransferase reaction
-
PII signal transduction protein
-
activates the adenylyltransferase reaction
-
signal transduction protein PII
-
adenylyltransferase reaction is activated by signal transduction protein PII, binding of signal transduction protein PII is favoured by glutamine and reduced by signal transduction protein PII-UMP, enzyme appears to have two distinct sites for signal transduction protein PII and signal transduction protein PII-UMP
signal transduction protein PII
-
binding of signal transduction protein PII is stimulated by glutamine
signal transduction protein PII
-
wild-tpye AT needs both signal transduction protein PII and Gln to stimulate full adenylylation activity
signal transduction protein PII
the adenylylation activity of AT-C is independent of PII (or PII-UMP), whereas in the intact enzyme PII is required for this activity
signal transduction protein 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
