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Literature summary extracted from

  • Weiss, L.A.; Stallings, C.L.
    Essential roles for Mycobacterium tuberculosis Rel beyond the production of (p)ppGpp (2013), J. Bacteriol., 195, 5629-5638.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
2.7.6.5 H344Y site-directed mutagenesis, the mutant enzyme shows no synthase activity Mycobacterium tuberculosis
2.7.6.5 H80A site-directed mutagenesis, the mutant enzyme shows no hydrolase activity Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.6.5 Mg2+ required Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.6.5 ATP + GDP Mycobacterium tuberculosis
-
 AMP + guanosine 3'-diphosphate 5'-diphosphate
-
 ?
2.7.6.5 ATP + GDP Mycobacterium tuberculosis ATCC 25618
-
 AMP + guanosine 3'-diphosphate 5'-diphosphate
-
 ?
2.7.6.5 ATP + GTP Mycobacterium tuberculosis
-
 AMP + guanosine 3'-diphosphate 5'-triphosphate
-
 ?
2.7.6.5 ATP + GTP Mycobacterium tuberculosis ATCC 25618
-
 AMP + guanosine 3'-diphosphate 5'-triphosphate
-
 ?
2.7.6.5 guanosine 3'-diphosphate 5'-diphosphate + H2O Mycobacterium tuberculosis
-
 GDP + diphosphate
-
 ?
2.7.6.5 guanosine 3'-diphosphate 5'-diphosphate + H2O Mycobacterium tuberculosis ATCC 25618
-
 GDP + diphosphate
-
 ?
2.7.6.5 guanosine 3'-diphosphate 5'-triphosphate + H2O Mycobacterium tuberculosis
-
 GTP + diphosphate
-
 ?
2.7.6.5 guanosine 3'-diphosphate 5'-triphosphate + H2O Mycobacterium tuberculosis ATCC 25618
-
 GTP + diphosphate
-
 ?
2.7.6.5 additional information Mycobacterium tuberculosis the enzyme transfers a diphosphate from ATP to GDP or GTP to synthesize guanosine 3'-diphosphate 5'-diphosphate (ppGpp) and guanosine 3'-diphosphate 5'-triphosphate (pppGpp), respectively. Enzyme RelMtb also encodes a second, distinct catalytic domain that hydrolyzes (p)ppGpp into diphosphate and GDP or GTP ?
-
 ?
2.7.6.5 additional information Mycobacterium tuberculosis ATCC 25618 the enzyme transfers a diphosphate from ATP to GDP or GTP to synthesize guanosine 3'-diphosphate 5'-diphosphate (ppGpp) and guanosine 3'-diphosphate 5'-triphosphate (pppGpp), respectively. Enzyme RelMtb also encodes a second, distinct catalytic domain that hydrolyzes (p)ppGpp into diphosphate and GDP or GTP ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.6.5 Mycobacterium tuberculosis P9WHG9 gene relA
-
2.7.6.5 Mycobacterium tuberculosis ATCC 25618 P9WHG9 gene relA
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.6.5 ATP + GDP
-
 Mycobacterium tuberculosis AMP + guanosine 3'-diphosphate 5'-diphosphate
-
 ?
2.7.6.5 ATP + GDP
-
 Mycobacterium tuberculosis ATCC 25618 AMP + guanosine 3'-diphosphate 5'-diphosphate
-
 ?
2.7.6.5 ATP + GTP
-
 Mycobacterium tuberculosis AMP + guanosine 3'-diphosphate 5'-triphosphate
-
 ?
2.7.6.5 ATP + GTP
-
 Mycobacterium tuberculosis ATCC 25618 AMP + guanosine 3'-diphosphate 5'-triphosphate
-
 ?
2.7.6.5 guanosine 3'-diphosphate 5'-diphosphate + H2O
-
 Mycobacterium tuberculosis GDP + diphosphate
-
 ?
2.7.6.5 guanosine 3'-diphosphate 5'-diphosphate + H2O
-
 Mycobacterium tuberculosis ATCC 25618 GDP + diphosphate
-
 ?
2.7.6.5 guanosine 3'-diphosphate 5'-triphosphate + H2O
-
 Mycobacterium tuberculosis GTP + diphosphate
-
 ?
2.7.6.5 guanosine 3'-diphosphate 5'-triphosphate + H2O
-
 Mycobacterium tuberculosis ATCC 25618 GTP + diphosphate
-
 ?
2.7.6.5 additional information the enzyme transfers a diphosphate from ATP to GDP or GTP to synthesize guanosine 3'-diphosphate 5'-diphosphate (ppGpp) and guanosine 3'-diphosphate 5'-triphosphate (pppGpp), respectively. Enzyme RelMtb also encodes a second, distinct catalytic domain that hydrolyzes (p)ppGpp into diphosphate and GDP or GTP Mycobacterium tuberculosis ?
-
 ?
2.7.6.5 additional information the enzyme transfers a diphosphate from ATP to GDP or GTP to synthesize guanosine 3'-diphosphate 5'-diphosphate (ppGpp) and guanosine 3'-diphosphate 5'-triphosphate (pppGpp), respectively. Enzyme RelMtb also encodes a second, distinct catalytic domain that hydrolyzes (p)ppGpp into diphosphate and GDP or GTP Mycobacterium tuberculosis ATCC 25618 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.6.5 (p)ppGpp synthetase
-
 Mycobacterium tuberculosis
2.7.6.5 Rel
-
 Mycobacterium tuberculosis
2.7.6.5 RelA
-
 Mycobacterium tuberculosis
2.7.6.5 RelMtb
-
 Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.6.5 ATP
-
 Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
2.7.6.5 malfunction Mycobacterium tuberculosis strains expressing the synthetase-dead RelMtb H344Y mutant do not persist in mice. Deletion of a second predicted (p)ppGpp synthetase has no effect on pathogenesis, demonstrating. Expression of an allele encoding the hydrolase-dead RelMtb mutant, RelMtb H80A, decreases the growth rate of Mycobacterium tuberculosis and changes the colony morphology of the bacteria. RelMtb H80A expression during acute or chronic Mycobacterium tuberculosis infection in mice is lethal to the infecting bacteria. Phenotypes, overview Mycobacterium tuberculosis
2.7.6.5 physiological function in Mycobacterium tuberculosis, the stringent response to amino acid starvation is mediated by the enzyme Rel (RelMtb), which transfers a diphosphate from ATP to GDP or GTP to synthesize guanosine 3'-diphosphate 5'-diphosphate (ppGpp) and guanosine 3'-diphosphate 5'-triphosphate (pppGpp), respectively. (p)ppGpp then influences numerous metabolic processes. RelMtb also encodes a second, distinct catalytic domain that hydrolyzes (p)ppGpp into diphosphate and GDP or GTP. RelMtb is required for chronic Mycobacterium tuberculosis infection in C57BL/6 mice. The RelMtb (p)ppGpp synthetase activity is required for maintaining bacterial titers during chronic infection, RelMtb is the major contributor to (p)ppGpp production during infection, RelMtb (p)ppGpp hydrolase activity is essential for acute and chronic infection of mice Mycobacterium tuberculosis