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2.7.7.89: [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase

This is an abbreviated version!
For detailed information about [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase, go to the full flat file.

Reaction

[glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine
+
phosphate
=
[glutamine synthetase]-L-tyrosine
 +
ADP

Synonyms

adenylyl(glutamine synthetase) hydrolase, adenylyl-[glutamine-synthetase] hydrolase, EC 3.1.4.15, GlnE, hydrolase adenylyl(glutamine synthetase), [glutamate-ammonia ligase]-adenylyl-L-tyrosine phosphorylase

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.89 [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase

Activating Compound

Activating Compound on EC 2.7.7.89 - [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase

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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
adenosine
-
activation by nucleotides, most efficient in presence of two different nucleotides
GTP
-
activation by nucleotides, most efficient in presence of two different nucleotides
ITP
-
activation by nucleotides, most efficient in presence of two different nucleotides
signal transduction protein PII
-
the protein activators PII and PII-UMP binding to the enzyme domain with the opposing activity, with intramolecular signal transduction by direct interactions between the N-terminal adenylyl-removing catalytic domain and the C-terminal adenylyltransferase catalytic domain
UMP
-
the protein activators PII and PII-UMP binding to the enzyme domain with the opposing activity, with intramolecular signal transduction by direct interactions between the N-terminal adenylyl-removing catalytic domain and the C-terminal adenylyltransferase catalytic domain
uridylated signal 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
-
uridylated signal transduction proteon PII
the deadenylylation activity of AT-N depends on PII-UMP
-
additional information
glutamine activates the adenylylation reaction of the AT-C domain, reaction of EC 2.7.7.42
-