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.
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
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Substrates Products
Substrates Products on EC 2.7.7.42 - [glutamine synthetase] adenylyltransferase
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REACTION DIAGRAM
ADP + glutamine synthetase
adenyl-[glutamine synthetase] + phosphate
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-
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r
ATP + glutamine synthetase
glutamine synthetase-AMP + diphosphate
the enzyme has two activities, adenylyl removase and adenylyl transferase, which are located in distinct catalytic domains that are separated by a regulatory domain
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-
?
ATP + [glutamine synthetase]-L-tyrosine
diphosphate + [glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
glutamine synthetase-AMP + phosphate
ADP + glutamine synthetase
the enzyme has two activities, adenylyl removase and adenylyl transferase, which are located in distinct catalytic domains that are separated by a regulatory domain
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-
?
[L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine + H2O
adenylate + [L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine
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-
-
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?
glutamine synthase + ADP
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adenylyl-removing reaction
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-
r
adenylyl-[glutamine synthase] + phosphate
glutamine synthase + ADP
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deadenylylation reaction
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r
adenylyl-[glutamine synthase] + phosphate
glutamine synthase + ADP
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adenylyl-removing reaction
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-
r
adenylated glutamine synthetase + diphosphate
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r
ATP + glutamine synthetase
adenylated glutamine synthetase + diphosphate
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?
diphosphate + [glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine
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-
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?
ATP + [glutamine synthetase]-L-tyrosine
diphosphate + [glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine
Escherichia coli B / ATCC 11303
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-
-
-
?
ATP + [glutamine synthetase]-L-tyrosine
diphosphate + [glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine
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-
-
?
ATP + [glutamine synthetase]-L-tyrosine
diphosphate + [glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine
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-
-
?
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
enzyme is responsible for regulation of [L-glutamate:ammonia ligase (ADP-forming)] activity
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?
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
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-
-
?
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
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-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
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-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
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-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
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enzyme is involved in the regulation of nitrogen assimilation
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r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
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inactivation of [L-glutamate:ammonia ligase (ADP-forming)] by attachment of the adenylyl moiety of ATP
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r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
inactivation of [L-glutamate:ammonia ligase (ADP-forming)] by attachment of the adenylyl moiety of ATP
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r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
Escherichia coli B / ATCC 11303
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-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
Escherichia coli B / ATCC 11303
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-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
Escherichia coli B / ATCC 11303
-
inactivation of [L-glutamate:ammonia ligase (ADP-forming)] by attachment of the adenylyl moiety of ATP
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r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
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-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
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-
r
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
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?
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
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-
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?
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
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-
-
-
?
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
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-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
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-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
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-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
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-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
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-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
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ADP, AMP, cAMP, UTP, CTP, ITP, NAD+ cannot replace ATP
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r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
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the site of adenylylation of the Mycobacterium tuberculosis [L-glutamate:ammonia ligase (ADP-forming)] by the Escherichia coli adenylyltransferase is Tyr406. [L-glutamate:ammonia ligase (ADP-forming)] is not adenylylated when obtained directly from Mycobacterium tuberculosis cultures that are not supplemented with glutamine. Upon the addition of glutamine to the cultures, the Mycobacterium tuberculosis enzyme becomes significantly adenylylated (about 30%)
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?
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
Escherichia coli B / ATCC 11303
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ADP, AMP, cAMP, UTP, CTP, ITP, NAD+ cannot replace ATP
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r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
Escherichia coli B / ATCC 11303
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-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
Escherichia coli B / ATCC 11303
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-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
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-
-
-
?
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
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-
-
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?
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
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-
-
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?
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
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-
-
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?
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
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-
-
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?
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
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-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
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-
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-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
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-
-
r
adenylyl-[glutamine synthase] + diphosphate
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adenylylation reaction
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r
glutamine synthase + ATP
adenylyl-[glutamine synthase] + diphosphate
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adenylyltransferase reaction
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r
glutamine synthase + ATP
adenylyl-[glutamine synthase] + diphosphate
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adenylyltransferase reaction
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r
glutamine synthase + ATP
adenylyl-[glutamine synthase] + diphosphate
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ATase primarily regulated by alpha-ketoglutarate, glutamine has no effect on neither the adenylylation nor the deadenylylation of glutamine synthetase, PII proteins only stimulate the adenylylation reaction
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r
?
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enzyme also catalyzes a phosphate exchange between ATP and diphosphate, which is also stimulated by glutamine
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?
additional information
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signal transduction system in nitrogen assimilation of Escherichia coli
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?
additional information
?
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enzyme is regulated by glutamine, 2-oxoglutarate and the regulatory enzymes PII and GlnK
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?
additional information
?
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the bifunctional adenylyltransferase ATase, product of glnE, catalyzes the adenylylation of glutamine synthetase and the deadenylylation of glutamine synthetase-AMP, reaction of EC 2.7.7.89. The adenylylation reaction is activated by PII signal transduction protein, while the deadenylylation reaction requires PII-UMP. Both of these reactions are stimulated by 2-ketoglutarate and ATP
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?
additional information
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Escherichia coli B / ATCC 11303
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enzyme also catalyzes a phosphate exchange between ATP and diphosphate, which is also stimulated by glutamine
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?