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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

ATP
+
[glutamine synthetase]-L-tyrosine
=
diphosphate
+
[glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine

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 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.42 [glutamine synthetase] adenylyltransferase

Inhibitors

Inhibitors on EC 2.7.7.42 - [glutamine synthetase] adenylyltransferase

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
3-phosphoglycerate
-
66% inhibition at 20 mM
4-Methyl-L-glutamate
-
-
6-diazo-5-oxonorleucine
-
-
alpha-ketoglutarate
-
in Rhodospirillum rubrum alpha-ketoglutarate inhibits the adenylylation activity of ATase
D-glutamine
-
-
diphosphate
DL-2-aminobutyric acid
-
-
glutamate
-
L- and D-isomer
glutamine
L-methionine
-
-
L-tryptophan
-
-
phosphate
-
-
PII signal transduction protein
-
adenylyl-removing activity
-
PII-UMP
-
adenylyltransferase activity
S-(2-Hydroxyethyl)-L-cysteine
-
-
signal transduction protein PII
-
inactivates the adenylyl-removing reaction
signal transduction protein PII-UMP
-
reaction is inhibited by signal transduction protein PII-UMP
sulfate
-
-
uridylated PII signal transduction protein
-
inhibits the adenylyltransferase reaction
-
uridylated 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
-
additional information
-
inactivation scheme
-