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
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.
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
mutant enzyme completely lacks adenylyl-removing activity but retains adenylyltransferase activity. Mutant exhibits significant basal adenylyltransferase activity in the absence of any activators
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
mutant enzyme completely lacks adenylyl-removing activity but retains adenylyltransferase activity. Mutant exhibits significant basal adenylyltransferase activity in the absence of any activators
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
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
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
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.
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
The glutamine synthetase deadenylylating enzyme system from Escherichia coli. Resolution into two components, specific nucleotide stimulation, and cofactor requirements
The regulation of Escherichia coli glutamine synthetase revisited: Role of 2-ketoglutarate in the regulation of glutamine synthetase adenylylation state
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