Literature summary for 2.7.7.42 extracted from

Jiang, P.; Pioszak, A.A.; Ninfa, A.J.
Structure-function analysis of glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49) of Escherichia coli (2007), Biochemistry, 46, 4117-4132.

Search for more literature for 2.7.7.42

Activating Compound

Activating Compound	Comment	Organism	Structure
alpha-ketoglutarate	0.02 mM	Escherichia coli
glutamine	activates the adenylyltransferase reaction	Escherichia coli
glutamine	binding of PII signal transduction to ATase is stimulated by glutamine	Escherichia coli
PII signal transduction protein	activates the adenylyltransferase reaction	Escherichia coli
signal transduction protein PII	binding of signal transduction protein PII is stimulated by glutamine	Escherichia coli

Cloned(Commentary)

Cloned (Comment)	Organism
cloned in Escherichia coli	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
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	Escherichia coli
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	Escherichia coli
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	Escherichia coli
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	Escherichia coli
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	Escherichia coli
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	Escherichia coli
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	Escherichia coli
additional information	truncation analysis shows that the protein contains a glutamine binding site and glutamine enhances the affinity for signal transduction protein PII	Escherichia coli
additional information	truncation analysis shows that the protein contains multiple binding sites for signal transduction protein PII and signal transduction protein PII-UMP	Escherichia coli
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	Escherichia coli
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	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
uridylated PII signal transduction protein	inhibits the adenylyltransferase reaction	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Escherichia coli
Mg2+	required	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-
Escherichia coli YMC10	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
ammonium sulfate fractionation, DE-52 column chromatography, Bio-Gel A0.5M gel filtration, and phenyl Sepharose column chromatography	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
adenylyl-[glutamine synthase] + phosphate	adenylyl-removing reaction	Escherichia coli	glutamine synthase + ADP	-	r
adenylyl-[glutamine synthase] + phosphate	adenylyl-removing reaction	Escherichia coli YMC10	glutamine synthase + ADP	-	r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]	-	Escherichia coli	diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)	-	?
ATP + [L-glutamate:ammonia ligase (ADP-forming)]	-	Escherichia coli YMC10	diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)	-	?
glutamine synthase + ATP	adenylyltransferase reaction	Escherichia coli	adenylyl-[glutamine synthase] + diphosphate	-	r
glutamine synthase + ATP	adenylyltransferase reaction	Escherichia coli YMC10	adenylyl-[glutamine synthase] + diphosphate	-	r

Synonyms

Synonyms	Comment	Organism
ATASE	-	Escherichia coli
glutamine synthetase adenylyltransferase	-	Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Escherichia coli

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)