Any feedback?
Information on EC 2.7.7.89 - [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase
for references in articles please use BRENDA:EC2.7.7.89Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.7.89 [glutamine synthetase]-adenylyl-L-tyrosine phosphorylaseIUBMB Comments
This bacterial enzyme removes an adenylyl group from a modified tyrosine residue of EC 6.3.1.2, glutamine synthetase. The enzyme is bifunctional, and also performs the adenylation of this residue (cf. EC 2.7.7.42, [glutamine synthetase] adenylyltransferase) [3,5]. The two activities are present on separate domains.
Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
[glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine
+
=
[glutamine synthetase]-L-tyrosine
+
Synonyms
adenylyl(glutamine synthetase) hydrolase, adenylyl-[glutamine-synthetase] hydrolase, EC 3.1.4.15, GlnE, hydrolase adenylyl(glutamine synthetase), [glutamate-ammonia ligase]-adenylyl-L-tyrosine phosphorylase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenylyl(glutamine synthetase) hydrolase
-
-
-
-
adenylyl-[glutamine-synthetase] hydrolase
-
-
-
-
EC 3.1.4.15
-
-
formerly
-
GlnE
hydrolase adenylyl(glutamine synthetase)
-
-
-
-
[glutamate-ammonia ligase]-adenylyl-L-tyrosine phosphorylase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
[glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine:phosphate adenylyltransferase
This bacterial enzyme removes an adenylyl group from a modified tyrosine residue of EC 6.3.1.2, glutamine synthetase. The enzyme is bifunctional, and also performs the adenylation of this residue (cf. EC 2.7.7.42, [glutamine synthetase] adenylyltransferase) [3,5]. The two activities are present on separate domains.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37288-22-5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O
?
-
activation of adenylated glutamine synthetase, EC 6.3.1.2, which is less active in catalyzing glutamine biosynthesis
-
-
?
adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O
adenylate + [L-glutamate:ammonia ligase (ADP-forming)]
[L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine + H2O
adenylate + [L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine
-
-
-
-
?
[L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine + phosphate
[L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine + ADP
-
-
-
-
?
additional information
?
-
-
the bifunctional adenylyltransferase ATase, product of glnE, catalyzes the adenylylation of glutamine synthetase and the deadenylylation of glutamine synthetase-AMP. 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-oxoglutarate and ATP
-
-
?
adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O
adenylate + [L-glutamate:ammonia ligase (ADP-forming)]
-
-
-
ir
adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O
adenylate + [L-glutamate:ammonia ligase (ADP-forming)]
-
-
the primary product may be ADP which is then degraded to AMP
ir
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O
?
-
activation of adenylated glutamine synthetase, EC 6.3.1.2, which is less active in catalyzing glutamine biosynthesis
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
-
activation by nucleotides, most efficient in presence of two different nucleotides
AMP
-
activation by nucleotides, most efficient in presence of two different nucleotides
ATP
-
activation by nucleotides, most efficient in presence of two different nucleotides
CTP
-
activation by nucleotides, most efficient in presence of two different nucleotides
UTP
-
activation by nucleotides, most efficient in presence of two different nucleotides
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
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
glutamine
-
the adenylyl-removing reaction is activated by PII-UMP and is inhibited by glutamine and by PII. 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
glutamine
-
glutamine inhibition of the adenylyl-removing activity involves intramolecular signaling between the adenylyltransferase and adenylyl-removing domains
signal transduction protein PII
-
the adenylyl-removing reaction is activated by PII-UMP and is inhibited by glutamine and by 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
signal transduction protein PII
the deadenylylation activity of AT-N is inhibited by PII
signal transduction protein PII
-
a tetrameric PIID molecule interacts with only one enzyme molecule at a time
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine
-
activation by nucleotides, most efficient in presence of two different nucleotides
GTP
-
activation by nucleotides, most efficient in presence of two different nucleotides
ITP
-
activation by nucleotides, most efficient in presence of two different nucleotides
signal transduction protein PII
-
the protein activators PII and PII-UMP binding to the enzyme domain with the opposing activity, with intramolecular signal transduction by direct interactions between the N-terminal adenylyl-removing catalytic domain and the C-terminal adenylyltransferase catalytic domain
UMP
-
the protein activators PII and PII-UMP binding to the enzyme domain with the opposing activity, with intramolecular signal transduction by direct interactions between the N-terminal adenylyl-removing catalytic domain and the C-terminal adenylyltransferase catalytic domain
uridylated signal transduction protein PII
-
the adenylyl-removing reaction is activated by PII-UMP and is inhibited by glutamine and by 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
-
uridylated signal transduction proteon PII
the deadenylylation activity of AT-N depends on PII-UMP
-
additional information
glutamine activates the adenylylation reaction of the AT-C domain, reaction of EC 2.7.7.42
-
2-oxoglutarate
activates the deadenylylation reaction catalysed by the N-domain
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.004
Adenylyl-[L-glutamate:ammonia ligase (ADP-forming)]
-
calculated as adenylyl groups removed from substrate
0.009
[L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine
-
pH 7.5, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8
-
80% of maximal activity at pH 6.5, 50% of maximal activity at pH 8.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
-
repressor MtrR the Neisseria gonorrhoeae mtrCDE efflux pump operon directly activates expression of GlnE, the dual functional adenyltransferase/deadenylase enzyme that modifies glutamine synthetase GlnA resulting in regulation of its role in glutamine biosynthesis
metabolism
-
repressor MtrR the Neisseria gonorrhoeae mtrCDE efflux pump operon directly activates expression of GlnE, the dual functional adenyltransferase/deadenylase enzyme that modifies glutamine synthetase GlnA resulting in regulation of its role in glutamine biosynthesis
-
physiological function
-
deletion of the deadenylylation domain has no apparent effect on growth or glutamine synthetase activity. In the presence of L-methionine sulfoximine, an inhibitor, and glutamine supplementation, a null mutant is able to grow similarly to the wild type. The GlnE mutant is able to survive and grow for extended periods in liquid medium, but not on solid medium, in the absence of glutamine synthetase inhibition
physiological function
-
glutamine synthetase adenylyltransferase regulates the activity of glutamine synthetase by adenylylation, reaction of EC 2.8.8.42, and deadenylylation in response to signals of nitrogen and carbon status
physiological function
The glutamine synthetase I activity of the glnE mutant is not down-regulated after an ammonium shock. However, the glutamine synthetase I activity of wild-type cells decreases to 60% of the original activity. GlnE mutants are glutamine prototrophic
physiological function
-
The glutamine synthetase I activity of the glnE mutant is not down-regulated after an ammonium shock. However, the glutamine synthetase I activity of wild-type cells decreases to 60% of the original activity. GlnE mutants are glutamine prototrophic
-
physiological function
-
deletion of the deadenylylation domain has no apparent effect on growth or glutamine synthetase activity. In the presence of L-methionine sulfoximine, an inhibitor, and glutamine supplementation, a null mutant is able to grow similarly to the wild type. The GlnE mutant is able to survive and grow for extended periods in liquid medium, but not on solid medium, in the absence of glutamine synthetase inhibition
-
physiological function
-
glutamine synthetase adenylyltransferase regulates the activity of glutamine synthetase by adenylylation, reaction of EC 2.8.8.42, and deadenylylation in response to signals of nitrogen and carbon status
-
Show AA Sequence and Transmembrane Helices (15554 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the N-terminal nucleotidyltransferase domain of the bifunctional enzyme contains the adenylyl-removing (AR) active site, and the C-terminal nucleotidyltransferase domain contains the adenylyltransferase (AT) active site. The enzyme contains a glutamine binding site, and glutamine increased the affinity for PII. The enzyme appears to contain multiple sites for the binding of PII and PII-UMP
additional information
-
the N-terminal nucleotidyltransferase domain of the bifunctional enzyme contains the adenylyl-removing (AR) active site, and the C-terminal nucleotidyltransferase domain contains the adenylyltransferase (AT) active site. The enzyme contains a glutamine binding site, and glutamine increased the affinity for PII. The enzyme appears to contain multiple sites for the binding of PII and PII-UMP
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the N-terminal domain of Escherichia coli adenylyltransferase, to 2.0 A resolution. The domain has a cluster of metal binding residues that are conserved in polbeta-like nucleotidyl transferases. The location of residues conserved in all adenylyltransferase sequences clusters around the active site
crystallization of a soluble N-terminal domain, residues 1-440, to 2.6 A resolution
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D173N/D175N
-
complete loss of adenylyl-removing activity, while adenylyltransferase activity is retained
D463N/P467A/L469G
-
mutant enzyme has approximately one-half to one-third of the adenylyl-removing activity observed with the wild-type enzyme, and this adenylyl-removing activity is inhibited by PII and by glutamine like the wild-type enzyme. The mutant enzyme also has approximately one-half to one-third of the adenylyltransferase activity when compared to the wild-type enzyme, and this activity is regulated normally by glutamine, PII, and PII-UMP
D701N/D703N
-
complete loss of adenylyltransferase activity, while adenylyl-removing activity is retained
R499A/R501A/D505N/P509A/L511G
-
mutant enzyme completely lacks adenylyl-removing activity but retains adenylyltransferase activity. Mutant exhibits significant basal adenylyltransferase activity in the absence of any activators
D173N/D175N
-
complete loss of adenylyl-removing activity, while adenylyltransferase activity is retained
-
D463N/P467A/L469G
-
mutant enzyme has approximately one-half to one-third of the adenylyl-removing activity observed with the wild-type enzyme, and this adenylyl-removing activity is inhibited by PII and by glutamine like the wild-type enzyme. The mutant enzyme also has approximately one-half to one-third of the adenylyltransferase activity when compared to the wild-type enzyme, and this activity is regulated normally by glutamine, PII, and PII-UMP
-
D701N/D703N
-
complete loss of adenylyltransferase activity, while adenylyl-removing activity is retained
-
R499A/R501A/D505N/P509A/L511G
-
mutant enzyme completely lacks adenylyl-removing activity but retains adenylyltransferase activity. Mutant exhibits significant basal adenylyltransferase activity in the absence of any activators
-
additional information
additional information
construcution of truncation mutants corresponding to amino acids 1-423 (AT-N) and 425-945 (AT-C). AT-N carries a deadenylylation activity and AT-C carries an adenylylation activity
additional information
expression of soluble N-terminal domain, residues 1-440, of the Escherichia coli adenylyl transferase responsible for deadenylylation activity. The domain is truncated at the end of a predicted helix and prior to a Q-linker, it is very soluble and stable. The construct has deadenylylation activity that is independent of the low nitrogen status indicator PII-UMP
additional information
-
truncated versions of ATase missing the C-terminal domain lacked both adenylyltransferase and the adenylyl-removing activity, suggesting a role for the C-terminal nucleotidyltransferase domain in both activities. The purified C-terminal nucleotidyltransferase domain and larger polypeptides containing this domain have significant basal AT activity, which is stimulated by glutamine. A truncated enzyme lacking amino acids 456-577 from the central region shows complete loss of adenylyl-removing activity, while adenylyltransferase activity is retained. Mutation converts signal transduction protein PII from an activator to an inhibitor
additional information
-
truncated versions of ATase missing the C-terminal domain lacked both adenylyltransferase and the adenylyl-removing activity, suggesting a role for the C-terminal nucleotidyltransferase domain in both activities. The purified C-terminal nucleotidyltransferase domain and larger polypeptides containing this domain have significant basal AT activity, which is stimulated by glutamine. A truncated enzyme lacking amino acids 456-577 from the central region shows complete loss of adenylyl-removing activity, while adenylyltransferase activity is retained. Mutation converts signal transduction protein PII from an activator to an inhibitor
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
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
repressor MtrR the Neisseria gonorrhoeae mtrCDE efflux pump operon directly activates expression of GlnE, the dual functional adenyltransferase/deadenylase enzyme that modifies glutamine synthetase GlnA resulting in regulation of its role in glutamine biosynthesis
repressor MtrR the Neisseria gonorrhoeae mtrCDE efflux pump operon directly activates expression of GlnE, the dual functional adenyltransferase/deadenylase enzyme that modifies glutamine synthetase GlnA resulting in regulation of its role in glutamine biosynthesis
-
repressor MtrR the Neisseria gonorrhoeae mtrCDE efflux pump operon directly activates expression of GlnE, the dual functional adenyltransferase/deadenylase enzyme that modifies glutamine synthetase GlnA resulting in regulation of its role in glutamine biosynthesis
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
the enzyme can be reconstituted from two purified polypeptides that comprise the N-terminal two-thirds of the protein and the C-terminal one-third of the protein. The reconstituted enzyme exhibits normal activation by signal transduction proteon PII. Properties of the reconstituted enzyme are consistent with the protein activators PII and PII-UMP binding to the enzyme domain with the opposing activity, with intramolecular signal transduction by direct interactions between the N-terminal adenylyl-removing catalytic domain and the C-terminal adenylyltransferase catalytic domain
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
development of a continuous fluorometric assay of the deadenylylation reaction and for measurement of uridylated signal transduction protein PII
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Heilmeyer, L.; Battig, F.; Holzer, H.
Characterization of a glutamine synthetase b activating (deadenylylating) enzyme system in Escherichia coli
Eur. J. Biochem.
9
259-262
1969
Escherichia coli
brenda
Shapiro, B.M.
The glutamine synthetase deadenylylating enzyme system from Escherichia coli. Resolution into two components, specific nucleotide stimulation, and cofactor requirements
Biochemistry
8
659-670
1969
Escherichia coli
brenda
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 (P30870)
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
Carroll, P.; Pashley, C.; Parish, T.
Functional analysis of GlnE, an essential adenylyl transferase in Mycobacterium tuberculosis
J. Bacteriol.
190
4894-4902
2008
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Son, H.; Rhee, S.
Cascade control of Escherichia coli glutamine synthetase. Purification and properties of PII protein and nucleotide sequence of its structural gene
J. Biol. Chem.
262
8690-8695
1987
Escherichia coli
brenda
Fink, D.; Falke, D.; Wohlleben, W.; Engels, A.
Nitrogen metabolism in Streptomyces coelicolor A3(2): Modification of glutamine synthetase I by an adenylyltransferase
Microbiology
145
2313-2322
1999
Streptomyces coelicolor (Q8CK02), Streptomyces coelicolor A3(2) (Q8CK02)
brenda
Van Heeswijk, W.; Hoving, S.; Molenaar, D.; Stegeman, B.; Kahn, D.; Westerhoff, H.
An alternative P(II) protein in the regulation of glutamine synthetase in Escherichia coli
Mol. Microbiol.
21
133-146
1996
Escherichia coli (P30870)
brenda
Xu, Y.; Wen, D.; Clancy, P.; Carr, P.; Ollis, D.; Vasudevan, S.
Expression, purification, crystallization, and preliminary X-ray analysis of the N-terminal domain of Escherichia coli adenylyl transferase
Protein Expr. Purif.
34
142-146
2004
Escherichia coli (P30870)
brenda
Johnson, P.J.; Shafer, W.M.
The transcriptional repressor, MtrR, of the mtrCDE efflux pump operon of Neisseria gonorrhoeae can also serve as an activator of "off target" gene (glnE) expression
Antibiotics
4
188-197
2015
Neisseria gonorrhoeae, Neisseria gonorrhoeae FA19
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.7.7.89)
html completed
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)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
