Literature summary for 6.3.5.2 extracted from

Abbott, J.L.; Newell, J.M.; Lightcap, C.M.; Olanich, M.E.; Loughlin, D.T.; Weller, M.A.; Lam, G.; Pollack, S.; Patton, W.A.
The effects of removing the GAT domain from E. coli GMP synthetase (2006), Protein J., 25, 483-491.

Cloned(Commentary)

Cloned (Comment)	Organism
cloning of ATPP/DD (a construct that contains the ATP-pyrophosphatase domain as well as the predicted dimerization domain), expression and purification of the corresponding protein, as both a His-tagged fusion protein (His-ATPP/DD) and as a non-fusion protein (NF-ATPP/DD). Both His-ATPP/DD and NF-ATPP/DD are active proteins, capable of catalyzing the conversion of XMP to GMP using exogenously added ammonia	Escherichia coli

Cloned (Comment)

Organism

cloning of ATPP/DD (a construct that contains the ATP-pyrophosphatase domain as well as the predicted dimerization domain), expression and purification of the corresponding protein, as both a His-tagged fusion protein (His-ATPP/DD) and as a non-fusion protein (NF-ATPP/DD). Both His-ATPP/DD and NF-ATPP/DD are active proteins, capable of catalyzing the conversion of XMP to GMP using exogenously added ammonia

Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
0.041	-	XMP	40°C, pH 8.0, NF-ATPP/DD	Escherichia coli
0.09	-	NH3	40°C, pH 8.0, His-ATPP/DD	Escherichia coli
0.096	-	XMP	40°C, pH 8.0, His-ATPP/DD	Escherichia coli
0.103	-	NH3	40°C, pH 8.0, wild-type enzyme	Escherichia coli
0.104	-	ATP	40°C, pH 8.0, wild-type enzyme	Escherichia coli
0.127	-	NH3	40°C, pH 8.0, NF-ATPP/DD	Escherichia coli
0.166	-	XMP	40°C, pH 8.0, wild-type enzyme	Escherichia coli
0.181	-	ATP	40°C, pH 8.0, NF-ATPP/DD	Escherichia coli
0.2	-	ATP	40°C, pH 8.0, His-ATPP/DD	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P04079	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + xanthosine 5'-phosphate + L-glutamine + H2O	GMP synthetase catalyzes the conversion of XMP to GMP. Ammonia, generated in the amino-terminal glutamine amidotransferase (GAT) domain, is transferred to the ATP-pyrophosphatase (ATPP) domain, where it attacks a highly reactive adenyl-XMP intermediate, leading to GMP formation	Escherichia coli	AMP + diphosphate + GMP + L-glutamate	-	?
ATP + xanthosine 5'-phosphate + NH3	ATPP/DD (a construct that contains the ATP-pyrophosphatase domain as well as the predicted dimerization domain) expressed as both a His-tagged fusion protein (His-ATPP/DD) and as a non-fusion protein (NF-ATPP/DD) is capable of catalyzing the conversion of XMP to GMP using exogenously added ammonia	Escherichia coli	AMP + diphosphate + GMP	-	?