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2.7.6.5: GTP diphosphokinase

This is an abbreviated version!
For detailed information about GTP diphosphokinase, go to the full flat file.

Word Map on EC 2.7.6.5

Reaction

ATP
+
GTP
=
AMP
 +
guanosine 3'-diphosphate 5'-triphosphate

Synonyms

(p)ppGpp synthase, (p)ppGpp synthetase, (p)ppGpp synthetase I, (p)ppGpp synthetase II, (p)ppGpp synthetase/hydrolase, alarmone synthetase, ATP-GTP 3'-diphosphotransferase, ATP:GTP 3'-pyrophosphotransferase, ATP:GTP pyrophosphoryl transferase, GPSI, GPSII, GTP pyrophosphokinase, guanosine 3',5'-polyphosphate synthase, guanosine 3',5'-polyphosphate synthetase, guanosine 5',3'-polyphosphate synthetase, guanosine pentaphosphate synthetase, ppGpp synthase I, Rel, Rel/Spo protein, RelA, RelMtb, RelMtb protein, RelP, RelSeq, RSH3, SAS 1, SAS 2, SAS1, SF, small alarmone synthase 1, small alarmone synthase 2, small alarmone synthetase 1, stringent factor, YjbM, YwaC

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.6 Diphosphotransferases
                2.7.6.5 GTP diphosphokinase

Engineering

Engineering on EC 2.7.6.5 - GTP diphosphokinase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D264G
site-directed mutagenesis, the mutation specifically abolishes (p)ppGpp synthetase activity without affecting other potential functions of the protein. Loss of the (p)ppGpp synthetase activity results in failure to grow on minimal medium and requirement for valine, leucine, isoleucine, threonine, and methionine, and a weaker requirement for arginine, histidine, and tryptophan addition
D72G
site-directed mutagenesis, the mutation specifically abolishes (p)ppGpp synthetase activity without affecting other potential functions of the protein. Loss of the (p)ppGpp synthetase activity results in failure to grow on minimal medium and requirement for valine, leucine, isoleucine, threonine, and methionine, and a weaker requirement for arginine, histidine, and tryptophan addition
D87G
site-directed mutagenesis, the mutation specifically abolishes (p)ppGpp synthetase activity without affecting other potential functions of the protein. Loss of the (p)ppGpp synthetase activity results in failure to grow on minimal medium and requirement for valine, leucine, isoleucine, threonine, and methionine, and a weaker requirement for arginine, histidine, and tryptophan addition
E324V
inactive in (p)ppGpp synthesis
G283E
mutation is located at the interface of synthesis domain and TGS domain. Mutant is deregulated, showing high (p)ppGpp synthetic and reduced (p)ppGpp hydrolytic activity
Y279E
mutation is located at the interface of synthesis domain and TGS domain. Mutant is inactive in (p)ppGpp synthesis in vitro, but not in vivo
D264G
-
site-directed mutagenesis, the mutation specifically abolishes (p)ppGpp synthetase activity without affecting other potential functions of the protein. Loss of the (p)ppGpp synthetase activity results in failure to grow on minimal medium and requirement for valine, leucine, isoleucine, threonine, and methionine, and a weaker requirement for arginine, histidine, and tryptophan addition
-
D72G
-
site-directed mutagenesis, the mutation specifically abolishes (p)ppGpp synthetase activity without affecting other potential functions of the protein. Loss of the (p)ppGpp synthetase activity results in failure to grow on minimal medium and requirement for valine, leucine, isoleucine, threonine, and methionine, and a weaker requirement for arginine, histidine, and tryptophan addition
-
D87G
-
site-directed mutagenesis, the mutation specifically abolishes (p)ppGpp synthetase activity without affecting other potential functions of the protein. Loss of the (p)ppGpp synthetase activity results in failure to grow on minimal medium and requirement for valine, leucine, isoleucine, threonine, and methionine, and a weaker requirement for arginine, histidine, and tryptophan addition
-
E324V
-
inactive in (p)ppGpp synthesis
-
G283E
-
mutation is located at the interface of synthesis domain and TGS domain. Mutant is deregulated, showing high (p)ppGpp synthetic and reduced (p)ppGpp hydrolytic activity
-
Y279E
-
mutation is located at the interface of synthesis domain and TGS domain. Mutant is inactive in (p)ppGpp synthesis in vitro, but not in vivo
-
E319Q
mutant lacks (p)ppGpp synthase activity but retains hydrolase activity
C633A
-
20fold decrease in activity
D632A
-
3.5fold decrease in activity
D81A
-
loss of hydrolytic activity with retention of synthesis
G241E
-
loss of synthetic activity and retention of hydrolysis
H344Y
H344Y
-
site-directed mutagenesis, the mutant enzyme shows no synthase activity
-
H80A
-
site-directed mutagenesis, the mutant enzyme shows no hydrolase activity
-
D264G
-
eliminates detectable synthetase activity without appreciably altering the hydrolase activity
E323Q
-
eliminates detectable synthetase activity without appreciably altering the hydrolase activity
additional information