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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Natural Substrates Products
Natural 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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r
ATP + glutamine synthetase
adenylated glutamine synthetase + diphosphate
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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)
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
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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?
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)
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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)
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
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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)
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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
?
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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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