Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.6.5 extracted from

  • Steinchen, W.; Schuhmacher, J.S.; Altegoer, F.; Fage, C.D.; Srinivasan, V.; Linne, U.; Marahiel, M.A.; Bange, G.
    Catalytic mechanism and allosteric regulation of an oligomeric (p)ppGpp synthetase by an alarmone (2015), Proc. Natl. Acad. Sci. USA, 112, 13348-13353.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.6.5

Cloned(Commentary)

Cloned (Comment) Organism
gene yjbM, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment) Organism
purified enzyme in presence of ATP and GTP, 1 week, X-ray diffraction structure determination and analysis at 2.94 A resolution Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information alarmone synthesis in SAS1 proceeds in a highly cooperative manner Bacillus subtilis
1.2
-
 GDP pH 7.5, 37°C, recombinant enzyme Bacillus subtilis
1.7
-
 GTP pH 7.5, 37°C, recombinant enzyme Bacillus subtilis
2
-
 guanosine 3'-diphosphate 5'-triphosphate pH 7.5, 37°C, recombinant enzyme Bacillus subtilis
3
-
 guanosine 3'-diphosphate 5'-diphosphate pH 7.5, 37°C, recombinant enzyme Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, binding structure analysis, overview Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + GDP Bacillus subtilis
-
 AMP + guanosine 3'-diphosphate 5'-diphosphate
-
 ?
ATP + GDP Bacillus subtilis 168
-
 AMP + guanosine 3'-diphosphate 5'-diphosphate
-
 ?
ATP + GTP Bacillus subtilis
-
 AMP + guanosine 3'-diphosphate 5'-triphosphate
-
 ?
ATP + GTP Bacillus subtilis 168
-
 AMP + guanosine 3'-diphosphate 5'-triphosphate
-
 ?
guanosine 3'-diphosphate 5'-diphosphate + H2O Bacillus subtilis
-
 GDP + diphosphate
-
 ?
guanosine 3'-diphosphate 5'-diphosphate + H2O Bacillus subtilis 168
-
 GDP + diphosphate
-
 ?
guanosine 3'-diphosphate 5'-triphosphate + H2O Bacillus subtilis
-
 GTP + diphosphate
-
 ?
guanosine 3'-diphosphate 5'-triphosphate + H2O Bacillus subtilis 168
-
 GTP + diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis O31611 gene yjbM
-
Bacillus subtilis 168 O31611 gene yjbM
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Bacillus subtilis

Reaction

Reaction Comment Organism Reaction ID
ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate the catalytic pathway of (p)ppGpp synthesis involves a sequentially ordered substrate binding, activation of ATP in a strained conformation, and transfer of diphosphate through a nucleophilic substitution (SN2) reaction. pppGpp, but not ppGpp, positively regulates the enzyme at an allosteric site Bacillus subtilis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + GDP
-
 Bacillus subtilis AMP + guanosine 3'-diphosphate 5'-diphosphate
-
 ?
ATP + GDP
-
 Bacillus subtilis 168 AMP + guanosine 3'-diphosphate 5'-diphosphate
-
 ?
ATP + GTP
-
 Bacillus subtilis AMP + guanosine 3'-diphosphate 5'-triphosphate
-
 ?
ATP + GTP
-
 Bacillus subtilis 168 AMP + guanosine 3'-diphosphate 5'-triphosphate
-
 ?
guanosine 3'-diphosphate 5'-diphosphate + H2O
-
 Bacillus subtilis GDP + diphosphate
-
 ?
guanosine 3'-diphosphate 5'-diphosphate + H2O
-
 Bacillus subtilis 168 GDP + diphosphate
-
 ?
guanosine 3'-diphosphate 5'-triphosphate + H2O
-
 Bacillus subtilis GTP + diphosphate
-
 ?
guanosine 3'-diphosphate 5'-triphosphate + H2O
-
 Bacillus subtilis 168 GTP + diphosphate
-
 ?
additional information the enzyme is bifunctional showing synthase activity forming ppGpp and pppGpp, and hydrolase activity with the two compounds resulting in formation of GTP or GDP and diphosphate Bacillus subtilis ?
-
 ?
additional information the enzyme is bifunctional showing synthase activity forming ppGpp and pppGpp, and hydrolase activity with the two compounds resulting in formation of GTP or GDP and diphosphate Bacillus subtilis 168 ?
-
 ?

Subunits

Subunits Comment Organism
homotetramer domain structure and three-dimensional homology modelling, sequence comparisons, crystal structure analysis, overview Bacillus subtilis

Synonyms

Synonyms Comment Organism
(p)ppGpp synthetase
-
 Bacillus subtilis
alarmone synthetase
-
 Bacillus subtilis
SAS1
-
 Bacillus subtilis
small alarmone synthetase 1
-
 Bacillus subtilis
YjbM
-
 Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
ATP binding structure analysis, overview Bacillus subtilis

General Information

General Information Comment Organism
evolution the enzyme belongs to the RSH superfamily, which controls concentrations of the alarmones (p)ppGpp (guanosine penta- or tetra-phosphate) Bacillus subtilis
additional information mechanism and allosteric regulation of the highly cooperative enzyme from Bacillus subtilis, overview. Analysis of the catalytic mechanism of (p)ppGpp synthesis by oligomeric and highly cooperative small alarmone synthetase 1 (SAS1) at atomic resolution, structural and biochemical analysis reveals that only pppGpp, but not ppGpp, positively affects the activity of the enzyme Bacillus subtilis
physiological function guanosine tetraphosphate (ppGpp) and guanosine pentaphosphate (pppGpp), collectively termed (p)ppGpp, act as alarmones that globally reprogram cellular physiology during various stress conditions. Enzymes of the RelA/SpoT homology (RSH) family synthesize (p)ppGpp by transferring diphosphate from ATP to GDP or GTP. ppGpp and pppGpp execute different functional roles Bacillus subtilis