3.1.7.2: guanosine-3',5'-bis(diphosphate) 3'-diphosphatase
This is an abbreviated version!
For detailed information about guanosine-3',5'-bis(diphosphate) 3'-diphosphatase, go to the full flat file.
Word Map on EC 3.1.7.2
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3.1.7.2
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rela
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alarmone
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rsh
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synthetases
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tetra
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sass
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di-gmp
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pppgpp-mediated
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enterococcal
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pppgpp0
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medicine
- 3.1.7.2
- rela
-
alarmone
- rsh
- synthetases
-
tetra
-
sass
-
di-gmp
-
pppgpp-mediated
-
enterococcal
-
pppgpp0
- medicine
Reaction
Synonyms
(p)ppGpp synthetase/hydrolase, (ppGpp)ase, 3',5'-bis(diphosphate) 3'-pyrophosphate hydrolase, guanosine-3',5'-bis(diphosphate) 3'-diphosphohydrolase, guanosine-3',5'-bis(diphosphate) 3'-pyrophosphatase, HDDC3, MESH1, metazoan SpoT homolog-1, penta-phosphate guanosine-3'-diphosphohydrolase, penta-phosphate guanosine-3'-pyrophosphohydrolase, ppGpp hydrolase, ppGpp phosphohydrolase, ppGpp-3'-pyrophosphohydrolase, pyrophosphatase, guanosine 3',5'-bis(diphosphate) 3'-, RelSeq
ECTree
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General Information
General Information on EC 3.1.7.2 - guanosine-3',5'-bis(diphosphate) 3'-diphosphatase
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malfunction
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Mesh1 deletion impairs starvation resistance in Drosophila, overview
physiological function
additional information
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crucial residues for the ppGpp hydrolysis activity of Mesh1 are Arg24, Glu65, Asp66 and Asn126
anti-sigma factor Rsd directly interacts with SpoT and stimulates its (p)ppGpp hydrolase activity. Dephosphorylated histidine-containing phosphocarrier protein HPr of the phosphoenolpyruvate-dependent sugar phosphotransferase system can antagonize the stimulatory effect of Rsd on SpoT (p)ppGpp hydrolase activity
physiological function
in vivo, under relaxed conditions, as well as in vitro, the C-terminal regulatory domain CTD inhibits synthetase activity but is not required for hydrolase activity. Under stringent conditions, the CTD is essential for (p)ppGpp synthesis. A mutant lacking the CTD exhibits net hydrolase activity when expressed in Staphylococcus aureus but net (p)ppGpp synthetase activity when expressed in Escherichia coli. The conserved TGS and DC motifs within the CTD are required for correct stringent response, whereas the conserved ACT motif is dispensable. The enzyme primarily exists in a synthetase-off/hydrolase-on state
physiological function
SpoT requires the ACT domain to efficiently hydrolyze (p)ppGpp. The phosphorylated version of EIIANtr interacts directly with the ACT and inhibits the hydrolase activity of SpoT
physiological function
the level of ppGpp controls the length of diauxic lag via control of the level of acetyl phosphate
physiological function
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SpoT requires the ACT domain to efficiently hydrolyze (p)ppGpp. The phosphorylated version of EIIANtr interacts directly with the ACT and inhibits the hydrolase activity of SpoT
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