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adenylyl-[glutamine synthase] + phosphate
glutamine synthase + ADP
ADP + glutamine synthetase
adenyl-[glutamine synthetase] + phosphate
-
-
-
-
r
ATP + glutamine synthetase
adenylated glutamine synthetase + diphosphate
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
-
-
?
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 synthase + ATP
adenylyl-[glutamine synthase] + diphosphate
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
-
-
?
[L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine + H2O
adenylate + [L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine
-
-
-
-
?
additional information
?
-
adenylyl-[glutamine synthase] + phosphate
glutamine synthase + ADP
-
adenylyl-removing reaction
-
-
r
adenylyl-[glutamine synthase] + phosphate
glutamine synthase + ADP
-
deadenylylation reaction
-
-
r
adenylyl-[glutamine synthase] + phosphate
glutamine synthase + ADP
-
adenylyl-removing reaction
-
-
r
ATP + glutamine synthetase
adenylated glutamine synthetase + diphosphate
-
-
-
r
ATP + glutamine synthetase
adenylated glutamine synthetase + diphosphate
-
-
-
-
?
ATP + [glutamine synthetase]-L-tyrosine
diphosphate + [glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine
-
-
-
-
?
ATP + [glutamine synthetase]-L-tyrosine
diphosphate + [glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine
-
-
-
-
?
ATP + [glutamine synthetase]-L-tyrosine
diphosphate + [glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine
-
-
-
?
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)
enzyme is responsible for regulation of [L-glutamate:ammonia ligase (ADP-forming)] activity
-
?
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)
-
-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
enzyme is involved in the regulation of nitrogen assimilation
-
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
-
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
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
-
-
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
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
-
-
r
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)
-
-
-
?
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)
-
-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
-
-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
-
-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
-
-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
-
-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
-
ADP, AMP, cAMP, UTP, CTP, ITP, NAD+ cannot replace ATP
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
-
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%)
-
-
?
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
-
ADP, AMP, cAMP, UTP, CTP, ITP, NAD+ cannot replace ATP
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
-
-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
-
-
-
r
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)
-
-
-
-
?
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)
-
-
-
-
?
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)
-
-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
-
-
-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
-
-
-
r
glutamine synthase + ATP
adenylyl-[glutamine synthase] + diphosphate
-
adenylylation reaction
-
-
r
glutamine synthase + ATP
adenylyl-[glutamine synthase] + diphosphate
-
adenylyltransferase reaction
-
-
r
glutamine synthase + ATP
adenylyl-[glutamine synthase] + diphosphate
-
adenylyltransferase reaction
-
-
r
glutamine synthase + ATP
adenylyl-[glutamine synthase] + diphosphate
-
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
-
-
r
additional information
?
-
-
enzyme also catalyzes a phosphate exchange between ATP and diphosphate, which is also stimulated by glutamine
-
-
?
additional information
?
-
-
signal transduction system in nitrogen assimilation of Escherichia coli
-
-
?
additional information
?
-
-
enzyme is regulated by glutamine, 2-oxoglutarate and the regulatory enzymes PII and GlnK
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme also catalyzes a phosphate exchange between ATP and diphosphate, which is also stimulated by glutamine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ADP + glutamine synthetase
adenyl-[glutamine synthetase] + phosphate
-
-
-
-
r
ATP + glutamine synthetase
adenylated glutamine synthetase + diphosphate
-
-
-
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
-
-
?
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
-
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
-
-
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
-
-
?
additional information
?
-
ATP + [glutamine synthetase]-L-tyrosine
diphosphate + [glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine
-
-
-
?
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)
enzyme is responsible for regulation of [L-glutamate:ammonia ligase (ADP-forming)] activity
-
?
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)
-
-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
enzyme is involved in the regulation of nitrogen assimilation
-
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
-
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
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
-
-
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
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
-
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
-
-
r
additional information
?
-
-
signal transduction system in nitrogen assimilation of Escherichia coli
-
-
?
additional information
?
-
-
enzyme is regulated by glutamine, 2-oxoglutarate and the regulatory enzymes PII and GlnK
-
-
?
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
-
PII signal transduction protein
-
PII-UMP
-
adenylyl-removing activity
signal transduction protein PII
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
-
1 mM
alpha-ketoglutarate
-
0.02 mM
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
-
activates the adenylyltransferase reaction
glutamine
-
binding of PII signal transduction to ATase is stimulated by glutamine
glutamine
-
adenylyltransferase activity
glutamine
activates the adenylylation reaction of the AT-C domain
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
-
required
L-glutamine
-
highly activating
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
-
activator of adenylylation
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
-
-
PII regulatory protein
-
PIIA is required
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
-
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 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
-
PII signal transduction protein
-
adenylyltransferase activity
-
signal transduction protein PII
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0009
adenylyl-[glutamine synthase]
-
adenylyl-removing activity, 0.00002 mM ATase, 1 mM alpha-ketoglutarate, 0.0005 mM signal transduction protein PII-UMP, 1 mM ATP, 5 mM potassium phosphate
-
0.0029 - 0.006
glutamine synthase
-
0.0032
glutamine synthetase
-
pH 7.5, 30Ā°C
-
0.33
potassium phosphate
-
adenylyl-removing activity, 0.00005 mM ATase, 1 mM alpha-ketoglutarate, 0.0005 mM signal transduction protein PII-UMP, 1 mM ATP, 0.00034 GS-AMP mM
0.005 - 1.1
[L-glutamate:ammonia ligase (ADP-forming)]
0.15
ATP
-
pH 7.6, 30Ā°C, in presence of glutamine
0.19
ATP
-
adenylation of Mycobacterium tuberculosis [L-glutamate:ammonia ligase (ADP-forming)] expressed in Escherichia coli
0.352
ATP
-
adenylation of Mycobacterium tuberculosis [L-glutamate:ammonia ligase (ADP-forming)]
0.75
ATP
-
adenylyltransferase activity, 0.0015 mM glutamine synthase, 0.05 mM alpha-ketoglutarate, 0.005 mM signal transduction protein PII, 0.0001 mM ATase
0.95
ATP
-
pH 7.6, 30Ā°C, in absence of glutamine
1.42
ATP
-
adenylyltransferase activity, 0.015 mM glutamine synthase, 0.05 mM alpha-ketoglutarate, 0.005 mM signal transduction protein PII, 0.0001 mM ATase
3.9
ATP
-
ATP in form of MgATP2-
0.0029
glutamine synthase
-
adenylyltransferase activity, 0.5 mM ATP, 0.05 mM alpha-ketoglutarate, 0.0005 mM signal transduction protein PII, 0.00008 mM ATase
-
0.0034
glutamine synthase
-
adenylyltransferase activity, 0.5 mM ATP, 0.05 mM alpha-ketoglutarate, 0.005 mM signal transduction protein PII, 0.0001 mM ATase
-
0.0035
glutamine synthase
-
adenylyltransferase activity, 0.5 mM ATP, 0.05 mM alpha-ketoglutarate, 0.0005 mM signal transduction protein PII, 0.0001 mM ATase
-
0.006
glutamine synthase
-
adenylyltransferase activity, 3.5 mM ATP, 0.05 mM alpha-ketoglutarate, 0.005 mM signal transduction protein PII, 0.00005 mM ATase
-
0.005
[L-glutamate:ammonia ligase (ADP-forming)]
-
pH 7.6, 30Ā°C
1.1
[L-glutamate:ammonia ligase (ADP-forming)]
-
pH 7.5, 22Ā°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0008 - 90
signal transduction protein PII
0.0008
signal transduction protein PII
-
inhibition of adenylyl-removing activity by signal transduction protein PII, 1 mM alpha-ketoglutarate, 0.0005 mM signal transduction protein PII-UMP, 50 mM glutamine, 0.00005 mM ATase
0.0012
signal transduction protein PII
-
inhibition of adenylyl-removing activity by signal transduction protein PII, 1 mM alpha-ketoglutarate, 0.0004 mM signal transduction protein PII-UMP, 50 mM glutamine, 0.00015 mM ATase
0.004
signal transduction protein PII
-
inhibition of adenylyl-removing activity by signal transduction protein PII, 1 mM alpha-ketoglutarate, 0.0005 mM signal transduction protein PII-UMP, 0.00005 mM ATase
0.008
signal transduction protein PII
-
inhibition of adenylyl-removing activity by signal transduction protein PII, 1 mM alpha-ketoglutarate, 0.0004 mM signal transduction protein PII-UMP, 0.00004 mM ATase
0.01
signal transduction protein PII
-
inhibition of adenylyl-removing activity by signal transduction protein PII, 1 mM alpha-ketoglutarate, 0.0001 mM signal transduction protein PII-UMP, 0.0001 mM ATase
0.08
signal transduction protein PII
-
inhibition of adenylyl-removing activity by signal transduction protein PII, 1 mM alpha-ketoglutarate, 0.01 mM signal transduction protein PII-UMP, 0.00002 mM ATase
5
signal transduction protein PII
-
inhibition of adenylyl-removing activity by signal transduction protein PII, 1 mM alpha-ketoglutarate, 0.0004 mM signal transduction protein PII-UMP, 0.01 mM signal transduction protein PII, 0.0002 mM ATase
9
signal transduction protein PII
-
inhibition of adenylyl-removing activity by signal transduction protein PII, 1 mM alpha-ketoglutarate, 0.0005 mM signal transduction protein PII-UMP, 0.001 mM signal transduction protein PII, 0.00005 mM ATase
23
signal transduction protein PII
-
inhibition of adenylyl-removing activity by signal transduction protein PII, 1 mM alpha-ketoglutarate, 0.0004 mM signal transduction protein PII-UMP, 0.00005 mM ATase
90
signal transduction protein PII
-
inhibition of adenylyl-removing activity by signal transduction protein PII, 1 mM alpha-ketoglutarate, 0.01 mM signal transduction protein PII-UMP, 0.0001 mM ATase
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D173N/D175N
-
inactivation of the N-terminal nucleotidyltransferase domain by mutation of both highly conserved aspartates, mutated enzyme shows adenylyltransferase activity but lacks adenylyl-removing activity
D463N/P467A/L469G
-
clustered point mutations in the central region of ATase, only 30-50% adenylyl-removing and adenylyltransferase activity of wild type enzyme, adenylyl-removing activity is inhibited by signal transduction protein PII and glutamine, adenylyltransferase activity is regulated by glutamine, signal transduction protein PII and signal transduction protein PII-UMP
D701N/D703N
-
inactivation of the C-terminal nucleotidyltransferase domain by mutation of both highly conserved aspartates, mutated enzyme shows adenylyl-removing activity but lacks adenylyltransferase activity
delata456-577
-
enzyme missing amino acids 456-577 from the central region of ATase lacks adenylyl-removing activity but retains adenylyltransferase activity, adenylyltransferase activity is inhibited by signal transduction protein PII and signal transduction protein PII-UMP
L525G/R527A/I528G
-
clustered point mutations in the central region of ATase, enzyme completely lacks adenylyl-removing activity but retains adenylyltransferase activity, adenylyltransferase activity is strongly enhanced by glutamine
R499A/R501A/D505N/P509A/L511G
-
clustered point mutations in the central region of ATase, enzyme completely lacks adenylyl-removing activity but retains adenylyltransferase activity, enzyme is inhibited by either signal transduction protein PII or signal transduction protein PII-UMP, adenylyltransferase activity is strongly enhanced by glutamine
R571A/P573A/L575G
-
clustered point mutations in the central region of ATase, enzyme shows approx. 12.5% of adenylyl-removing activity of wild-type enzyme, adenylyl-removing activity is inhibited by glutamine and signal transduction protein PII, adenylyltransferase activity is strongly activated by glutamine
D438Y/R657S/S684K
-
temperature-sensitive mutant
D720A
-
mutation in the adenylylation domain, compromises activity. Strain shows reduced growth rates in the low-ammonia- and glutamine-containing media
D732A
-
mutation in the adenylylation domain, mutation does not completely abrogate the enzyme activity
V921Q
-
temperature-sensitive mutant
D438Y/R657S/S684K
-
temperature-sensitive mutant
-
D720A
-
mutation in the adenylylation domain, compromises activity. Strain shows reduced growth rates in the low-ammonia- and glutamine-containing media
-
D732A
-
mutation in the adenylylation domain, mutation does not completely abrogate the enzyme activity
-
V921Q
-
temperature-sensitive mutant
-
additional information
construction of null mutant LNDELTAglnE strain with chromosomal deletion of gene glnE, the mutant does not respond to nitrogen level like the wild-type, the mutant shows a higher [L-glutamate:ammonia ligase (ADP-forming)] activity level compared to the wild-type when grown in nitrogen-rich medium due to upregulation of glnA
additional information
-
construction of null mutant LNDELTAglnE strain with chromosomal deletion of gene glnE, the mutant does not respond to nitrogen level like the wild-type, the mutant shows a higher [L-glutamate:ammonia ligase (ADP-forming)] activity level compared to the wild-type when grown in nitrogen-rich medium due to upregulation of glnA
additional information
-
all C-terminal truncation constructs are dependent on Gln for full adenylylation activity
additional information
-
mAbs to AT are used to demonstrate that signal transduction protein PII and signal transduction protein PII-UMP probably bind in the central regulatory domain between residues 466 and 507 to stimulate the adenylylation and deadenylylation reactions, respectively
additional information
-
several truncated versions of ATase are created, indicating that the N-terminal nucleotidyltransferase domain contains the adenylyl-removing active site and the C-terminal nucleotidyltransferase domain contains the adenylyltransferase active site
additional information
-
solubility and enzymatic analysis of several deletion constructs of AT show that AT has three domains: the two activity domains and a central, probably regulatory, domain connected by interdomain Q-linkers (N-Q1-R-Q2-C), the various constructs which have the opposing domain removed, all retain their activity in the absence of their nitrogen status indicator signal transduction protein PII or signal transduction protein PII-UMP
additional information
-
truncated versions missing the C-terminal nucleotidyltransferase domain lacks both adenylyltransferase and adenylyl-removing activity, suggesting a role of the C-terminal nucleotidyltransferase domain in both activities
additional information
-
truncation analysis shows that the protein contains a glutamine binding site and glutamine enhances the affinity for signal transduction protein PII
additional information
-
truncation analysis shows that the protein contains multiple binding sites for signal transduction protein PII and signal transduction protein PII-UMP
additional information
construcution of truncation mutants corresponding to amino acids 1Ā423 (AT-N) and 425Ā945 (AT-C). AT-N carries a deadenylylation activity, reaction of EC 2.7.7.89, and AT-C carries an adenylylation activity
additional information
-
sequences for the active sites for adenylylation and deadenylylation as in Escherichia coli are also present in Rhodospirillum rubrum, between amino acids 107-329 and 632-849, respectively, however a Q-linker as in Escherichia coli can not be identified
additional information
-
the C-terminal part of the protein between amino acids 1006-1149 shows high similarity to an Escherichia coli bacterioferritin comigratory protein (BCP)
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