Any feedback?
Information on EC 2.7.7.42 - [glutamine synthetase] adenylyltransferase and Organism(s) Escherichia coli and UniProt Accession P30870
for references in articles please use BRENDA:EC2.7.7.42Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.7.42 [glutamine synthetase] adenylyltransferaseIUBMB Comments
This bacterial enzyme adenylates a tyrosine residue of EC 6.3.1.2, glutamine synthetase. The enzyme is bifunctional, and also catalyses a reaction that removes the adenyl group from the modified tyrosine residue (cf. EC 2.7.7.89, [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase) [7,8]. The two activities are present on separate domains.
Specify your search results
Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
+
=
+
+
[glutamine synthetase]-L-tyrosine
=
+
[glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine
Synonyms
adenylyltransferase, glutamine synthetase adenylyltransferase, glutamine-synthetase adenylyltransferase, atp:glutamine synthetase adenylyltransferase, glutamine synthetase adenylyl transferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATP:[L-glutamate:ammonia ligase (ADP-forming)] adenylyl transferase
-
adenosine triphosphate:glutamine synthetase adenylyltransferase
-
-
-
-
adenylyltransferase, glutamine synthetase
-
-
-
-
ATP:glutamine synthetase adenylyltransferase
-
-
-
-
glutamine synthetase adenylyltransferase
glutamine-synthetase adenylyltransferase
-
-
-
-
[glutamate-ammonia-ligase] adenylyltransferase
-
-
-
-
glutamine synthetase adenylyltransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + [glutamine synthetase]-L-tyrosine = diphosphate + [glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:[glutamine synthetase]-L-tyrosine adenylyltransferase
This bacterial enzyme adenylates a tyrosine residue of EC 6.3.1.2, glutamine synthetase. The enzyme is bifunctional, and also catalyses a reaction that removes the adenyl group from the modified tyrosine residue (cf. EC 2.7.7.89, [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase) [7,8]. The two activities are present on separate domains.
CAS REGISTRY NUMBER
COMMENTARY
9077-66-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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
-
-
?
ADP + glutamine synthetase
adenyl-[glutamine synthetase] + phosphate
-
-
-
-
r
ATP + glutamine synthetase
adenylated glutamine synthetase + diphosphate
-
-
-
-
?
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)
[L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine + H2O
adenylate + [L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine
-
-
-
-
?
adenylyl-[glutamine synthase] + phosphate
glutamine synthase + ADP
-
adenylyl-removing reaction
-
-
r
adenylyl-[glutamine synthase] + phosphate
glutamine synthase + ADP
-
deadenylylation reaction
-
-
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)
-
-
-
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)
-
-
-
?
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%)
-
-
?
glutamine synthase + ATP
adenylyl-[glutamine synthase] + diphosphate
-
adenylylation reaction
-
-
r
glutamine synthase + ATP
adenylyl-[glutamine synthase] + diphosphate
-
adenylyltransferase 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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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
-
-
?
ADP + glutamine synthetase
adenyl-[glutamine synthetase] + phosphate
-
-
-
-
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)
-
-
-
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
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
signal transduction protein PII
-
inactivates the adenylyl-removing reaction
signal transduction protein PII-UMP
-
reaction is inhibited by signal transduction protein PII-UMP
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
-
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
ATP
-
inhibitory above 1 mM in presence of glutamine, not related to Mg2+ concentration
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
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
-
binding of PII signal transduction to ATase is stimulated by glutamine
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
-
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
-
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
-
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 signal transduction protein
-
0.0004 mM, activates the adenylyltransferase reaction
-
PII signal transduction protein
-
activates the adenylyltransferase reaction
-
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 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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
0.33
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
0.19
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
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
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
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 9.8
-
pH 5.5: about 50% of activity maximum, pH 9.8: about 35% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the adenylyltransferase is part of the cascade that regulates the activity of glutamine synthetase, a key compound of the cells machinery for the uptake of ammonia
physiological function
-
the adenylyltransferase and its substrate glutamine synthetase are part of a signal transduction system that includes two additional proteins, uridylyltransferase/uridylyl-removing enzyme and the PII protein
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
114000
-
1 * 114000, high speed sedimentation study of the enzyme in 6 M guanidine-HCl
64000
-
low and high speed sedimentation equilibrium, 115000 MW enzyme form is slowly converted during storage at 4°C to a smaller protein that is active only in adenylylation, not in deadenylylation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
1 * 114000, high speed sedimentation study of the enzyme in 6 M guanidine-HCl
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of the N-terminal domain, residues 1-440, containing the regulatory and the adenylyl transferase domains, to 2.4 A resolution. Deduction of a model of the complete enzyme and a model for the complex with glutamine synthetase and the nitrogen signal transduction protein PII
the structure of the C-terminal fragment, containing residues 449-946, of glutamine synthetase adenylyl transferase is determined to a resolution of 2.4 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
additional information
construcution of truncation mutants corresponding to amino acids 1423 (AT-N) and 425945 (AT-C). AT-N carries a deadenylylation activity, reaction of EC 2.7.7.89, and AT-C carries an adenylylation activity
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
bovine serum albumin, above 1 mg/ml, prevents inactivation at 4°C and 25°C and aggregation
-
considerably less stable in Tris or imidazole buffer than in a magnesium phosphate buffer
-
no stabilization by ATP, CTP, Mn2+, glutamine, cysteine or mercaptoethanol each at 20 mM, 2 mM DTT, 20% glycerol, sucrose, polyethyleneglycol or urea at 1 M
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, purified enzyme, stored after quick freezing with liquid N2, potassium phosphate buffer, 10-100 mM, pH 7.6, 1 mM MgCl2, stable for months at enzyme concentration above 0.1 mg/ml
-
4°C, enzyme solution of 3 mg/ml, loss of 50% activity within 30 days, the activity declines faster with more diluted enzyme solutions
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation, DE-52 column chromatography, Bio-Gel A0.5M gel filtration, and phenyl Sepharose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene GlnE is cotranscribed with another gene, orfXE. All three Gln regulatory genes, uridylyl-transferase (GlnD), the PII protein (GlnB), and adenyly I-transferase (gInE) are constitutively expressed at a low level, i.e. their expression is independent of the nitrogen status and the RNA polymerase sigma factor
gene expression is slightly repressed under nitrogen-excess conditions, and the repression is more pronounced under excess nitrogen plus carbon-limiting conditions. Variations in the concentration of uridylyltransferase and adenylyltransferase also affect the rate of glutamine synthetase synthesis
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ebner, E.; Wolf, D.; Gancedo, C.; Elssser, S.; Holzer, H.
ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties
Eur. J. Biochem.
14
535-544
1970
Escherichia coli, Escherichia coli B / ATCC 11303
Wolf, D.; Ebner, E.; Hinze, H.
Inactivation, stabilization and some properties of ATP: glutamine synthetase adenylyltransferase from Escherichia coli B
Eur. J. Biochem.
25
239-244
1972
Escherichia coli, Escherichia coli B / ATCC 11303
Wolf, D.H.; Ebner, E.
Studies on the reaction mechanism of adenosine triphosphate: glutamine synthetase adenylyltransferase from Escherichia coli B. Conformational changes elicited by effectors and substrates: reactivity of sulfhydryl groups
J. Biol. Chem.
247
4208-4212
1972
Escherichia coli
Wohlhueter, R.M.; Ebner, E.; Wolf, D.H.
Studies on the reaction mechanism of adenosine triphosphate: glutamine synthetase adenylyltransferase from Escherichia coli B. Evidence for an ordered mechanism
J. Biol. Chem.
247
4213-4218
1972
Escherichia coli, Escherichia coli B / ATCC 11303
Rhee, S.G.; Park, R.; Wittenberger, M.
New enzymic assays for glutamine synthetase adenylytransferase and its regulatory protein PIIA
Anal. Biochem.
88
174-185
1978
Escherichia coli, Pseudomonas putida, Salmonella enterica subsp. enterica serovar Typhimurium
Caban, C.E.; Ginsburg, A.
Glutamine synthetase adenylyltransferase from Escherichia coli: purification and physical and chemical properties
Biochemistry
15
1569-1580
1976
Escherichia coli
Atkinson, M.R.; Ninfa, A.J.
Role of the GlnK signal transduction protein in the regulation of nitrogen assimilation in Escherichia coli
Mol. Microbiol.
29
431-447
1998
Escherichia coli
Xu, Y.; Wen, D.; Brown, C.; Chen, C.J.; Carr, P.D.; Ollis, D.L.; Vasudevan, S.G.
Expression, purification and crystallization of the C-terminal domain of Escherichia coli adenylyltransferase
Acta Crystallogr. Sect. F
F61
663-665
2005
Escherichia coli
Mehta, R.; Pearson, J.T.; Mahajan, S.; Nath, A.; Hickey, M.J.; Sherman, D.R.; Atkins, W.M.
Adenylylation and catalytic properties of Mycobacterium tuberculosis glutamine synthetase expressed in Escherichia coli versus Mycobacteria
J. Biol. Chem.
279
22477-22482
2004
Escherichia coli
Xu, Y.; Zhang, R.; Joachimiak, A.; Carr, P.D.; Huber, T.; Vasudevan, S.G.; Ollis, D.L.
Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase
Structure
12
861-869
2004
Escherichia coli
Jiang, P.; Pioszak, A.A.; Ninfa, A.J.
Structure-function analysis of glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49) of Escherichia coli
Biochemistry
46
4117-4132
2007
Escherichia coli, Escherichia coli YMC10
Jiang, P.; Mayo, A.E.; Ninfa, A.J.
Escherichia coli glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49): kinetic characterization of regulation by PII, PII-UMP, glutamine, and alpha-ketoglutarate
Biochemistry
46
4133-4146
2007
Escherichia coli
Clancy, P.; Xu, Y.; van Heeswijk, W.C.; Vasudevan, S.G.; Ollis, D.L.
The domains carrying the opposing activities in adenylyltransferase are separated by a central regulatory domain
FEBS J.
274
2865-2877
2007
Escherichia coli
Jiang, P.; Ninfa, A.J.
Reconstitution of Escherichia coli glutamine synthetase adenylyltransferase from N-terminal and C-terminal fragments of the enzyme
Biochemistry
48
415-423
2009
Escherichia coli
Xu, Y.; Carr, P.D.; Vasudevan, S.G.; Ollis, D.L.
Structure of the adenylylation domain of E. coli glutamine synthetase adenylyl transferase: Evidence for gene duplication and evolution of a new active site
J. Mol. Biol.
396
773-784
2010
Escherichia coli (P30870), Escherichia coli
Jiang, P.; Peliska, J.; Ninfa, A.
The regulation of Escherichia coli glutamine synthetase revisited: Role of 2-ketoglutarate in the regulation of glutamine synthetase adenylylation state
Biochemistry
37
12802-12810
1998
Escherichia coli
Rhee, S.; Park, S.; Koo, J.
The role of adenylyltransferase and uridylyltransferase in the regulation of glutamine synthetase in Escherichia coli
Curr. Top. Cell. Regul.
27
221-232
1985
Escherichia coli
Jaggi, R.; Van Heeswijk, W.; Westerhoff, H.; Ollis, D.; Vasudevan, S.
The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction
EMBO J.
16
5562-5571
1997
Escherichia coli (P30870)
EXTERNAL LINKS (specific for EC-Number 2.7.7.42)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
