Information on EC 2.7.7.89 - [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.7.89
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RECOMMENDED NAME
GeneOntology No.
[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
37288-22-5
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O
?
show the reaction diagram
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activation of adenylated glutamine synthetase, EC 6.3.1.2, which is less active in catalyzing glutamine biosynthesis
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adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O
adenylate + [L-glutamate:ammonia ligase (ADP-forming)]
show the reaction diagram
[L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine + H2O
adenylate + [L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine
show the reaction diagram
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?
[L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine + phosphate
[L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine + ADP
show the reaction diagram
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?
additional information
?
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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
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O
?
show the reaction diagram
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activation of adenylated glutamine synthetase, EC 6.3.1.2, which is less active in catalyzing glutamine biosynthesis
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
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activation by nucleotides, most efficient in presence of two different nucleotides
AMP
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activation by nucleotides, most efficient in presence of two different nucleotides
ATP
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activation by nucleotides, most efficient in presence of two different nucleotides
CTP
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activation by nucleotides, most efficient in presence of two different nucleotides
UTP
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activation by nucleotides, most efficient in presence of two different nucleotides
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
arsenate
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activation
Mg2+
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activation
Mn2+
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activation
phosphate
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activation
additional information
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not activated by Ca2+, Cd2+, Zn2+, Ba2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
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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
diphosphate
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glutamate
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glutamine
signal transduction protein PII
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
adenosine
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activation by nucleotides, most efficient in presence of two different nucleotides
GTP
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activation by nucleotides, most efficient in presence of two different nucleotides
ITP
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activation by nucleotides, most efficient in presence of two different nucleotides
signal transduction protein PII
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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
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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
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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
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uridylated signal transduction proteon PII
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the deadenylylation activity of AT-N depends on PII-UMP
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additional information
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glutamine activates the adenylylation reaction of the AT-C domain, reaction of EC 2.7.7.42
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004
Adenylyl-[L-glutamate:ammonia ligase (ADP-forming)]
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calculated as adenylyl groups removed from substrate
0.33
phosphate
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pH 7.5, 30°C
0.009
[L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine
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pH 7.5, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
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80% of maximal activity at pH 6.5, 50% of maximal activity at pH 8.0
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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
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crystallization of a soluble N-terminal domain, residues 1-440, to 2.6 A resolution
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 2 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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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
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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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D173N/D175N
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complete loss of adenylyl-removing activity, while adenylyltransferase activity is retained
D463N/P467A/L469G
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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
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complete loss of adenylyltransferase activity, while adenylyl-removing activity is retained
R499A/R501A/D505N/P509A/L511G
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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
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complete loss of adenylyl-removing activity, while adenylyltransferase activity is retained
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D463N/P467A/L469G
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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
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D701N/D703N
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complete loss of adenylyltransferase activity, while adenylyl-removing activity is retained
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R499A/R501A/D505N/P509A/L511G
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mutant enzyme completely lacks adenylyl-removing activity but retains adenylyltransferase activity. Mutant exhibits significant basal adenylyltransferase activity in the absence of any activators
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additional information
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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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development of a continuous fluorometric assay of the deadenylylation reaction and for measurement of uridylated signal transduction protein PII
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