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Literature summary extracted from

  • Murdeshwar, M.S.; Chatterji, D.
    MS_RHII-RSD, a dual-function RNase HII-(p)ppGpp synthetase from Mycobacterium smegmatis (2012), J. Bacteriol., 194, 4003-4014.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.6.5 expressed in Escherichia coli BL21(DE3) cells Mycolicibacterium smegmatis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.6.5 Mg2+ the enzyme shows a marked decrease in guanosine tetraphosphate synthesis activity with increasing Mg2+ ion concentration Mycolicibacterium smegmatis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.6.5 1.163
-
 GTP in 50 mM HEPES, pH 7.5, at 37°C Mycolicibacterium smegmatis
2.7.6.5 1.532
-
 GDP in 50 mM HEPES, pH 7.5, at 37°C Mycolicibacterium smegmatis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.6.5 Mg2+ the enzyme exploits a single Mg2+ ion to catalyze guanosine 3'-diphosphate 5'-triphosphate synthesis Mycolicibacterium smegmatis

Organism

EC Number Organism UniProt Comment Textmining
2.7.6.5 Mycolicibacterium smegmatis
-
-
-
2.7.6.5 Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.6.5 Ni-NTA column chromatography, and gel filtration Mycolicibacterium smegmatis

Renatured (Commentary)

EC Number Renatured (Comment) Organism
2.7.6.5 the purified enzyme is renatured by stepwise dialysis in buffers containing sequentially decreasing concentrations of urea (50mM Tris-HCl, pH 7.9 at 4°C, 150 mM NaCl, 100 mM imidazole, and 4 M, 2 M, and 0 M urea, in that order) Mycolicibacterium smegmatis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.6.5 ATP + GDP the enzyme utilizes GDP less efficiently than GTP Mycolicibacterium smegmatis AMP + guanosine 3',5'-bis-diphosphate
-
 ?
2.7.6.5 ATP + GDP the enzyme utilizes GDP less efficiently than GTP Mycolicibacterium smegmatis mc(2)155 / ATCC 700084 AMP + guanosine 3',5'-bis-diphosphate
-
 ?
2.7.6.5 ATP + GTP the enzyme uses GTP approximately twice as well as GDP Mycolicibacterium smegmatis AMP + guanosine 3'-diphosphate 5'-triphosphate
-
 ?
2.7.6.5 ATP + GTP the enzyme uses GTP approximately twice as well as GDP Mycolicibacterium smegmatis mc(2)155 / ATCC 700084 AMP + guanosine 3'-diphosphate 5'-triphosphate
-
 ?
2.7.6.5 additional information the enzyme also possesses a potent Mn2+-dependent guanosine tetraphosphate hydrolysis activity, with complete hydrolysis to GDP and diphosphate Mycolicibacterium smegmatis ?
-
 ?
2.7.6.5 additional information the enzyme also possesses a potent Mn2+-dependent guanosine tetraphosphate hydrolysis activity, with complete hydrolysis to GDP and diphosphate Mycolicibacterium smegmatis mc(2)155 / ATCC 700084 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.6.5 (p)ppGpp synthetase
-
 Mycolicibacterium smegmatis
2.7.6.5 Rel
-
 Mycolicibacterium smegmatis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.6.5 73
-
 GDP in 50 mM HEPES, pH 7.5, at 37°C Mycolicibacterium smegmatis
2.7.6.5 127
-
 GTP in 50 mM HEPES, pH 7.5, at 37°C Mycolicibacterium smegmatis

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.7.6.5 Mycolicibacterium smegmatis calculated from amino acid sequence
-
 8.1