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Literature summary extracted from

  • Nomura, Y.; Izumi, A.; Fukunaga, Y.; Kusumi, K.; Iba, K.; Watanabe, S.; Nakahira, Y.; Weber, A.P.; Nozawa, A.; Tozawa, Y.
    Diversity in guanosine 3,5-bisdiphosphate (ppGpp) sensitivity among guanylate kinases of bacteria and plants (2014), J. Biol. Chem., 289, 15631-15641.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.4.8 recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Arabidopsis thaliana
2.7.4.8 recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Bacillus subtilis
2.7.4.8 recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Escherichia coli
2.7.4.8 recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Lathyrus oleraceus
2.7.4.8 recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Oryza sativa Japonica Group
2.7.4.8 recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Saccharomyces cerevisiae
2.7.4.8 recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Synechococcus elongatus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.4.8 guanosine 3',5'-bisdiphosphate specific inhibition of the organellar isozyme Arabidopsis thaliana
2.7.4.8 guanosine 3',5'-bisdiphosphate specific inhibition of the isozyme Bacillus subtilis
2.7.4.8 guanosine 3',5'-bisdiphosphate specific inhibition of the organellar isozyme Lathyrus oleraceus
2.7.4.8 guanosine 3',5'-bisdiphosphate specific inhibition of the organellar isozyme Oryza sativa Japonica Group
2.7.4.8 additional information no inhibition of the cytosolic isozyme by guanosine 3',5'-bisdiphosphate Escherichia coli
2.7.4.8 additional information no inhibition of the cytosolic isozyme by guanosine 3',5'-bisdiphosphate Lathyrus oleraceus
2.7.4.8 additional information no inhibition of the cytosolic isozyme by guanosine 3',5'-bisdiphosphate Oryza sativa Japonica Group
2.7.4.8 additional information no inhibition of the cytosolic isozyme by guanosine 3',5'-bisdiphosphate Saccharomyces cerevisiae
2.7.4.8 additional information no inhibition of the cytosolic isozyme by guanosine 3',5'-bisdiphosphate Synechococcus elongatus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.4.8 0.073
-
 GMP recombinant chloroplast isozyme, pH 7.5, 30°C Oryza sativa Japonica Group
2.7.4.8 0.156
-
 GMP recombinant cytosolic isozyme, pH 7.5, 30°C Escherichia coli
2.7.4.8 0.165
-
 GMP recombinant isozyme, pH 7.5, 30°C Bacillus subtilis
2.7.4.8 0.202
-
 GMP recombinant cytosolic isozyme, pH 7.5, 30°C Oryza sativa Japonica Group

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.4.8 chloroplast
-
 Oryza sativa Japonica Group 9507
-
2.7.4.8 chloroplast
-
 Arabidopsis thaliana 9507
-
2.7.4.8 chloroplast
-
 Lathyrus oleraceus 9507
-
2.7.4.8 cytosol
-
 Escherichia coli 5829
-
2.7.4.8 cytosol
-
 Synechococcus elongatus 5829
-
2.7.4.8 cytosol
-
 Lathyrus oleraceus 5829
-
2.7.4.8 cytosol
-
 Oryza sativa Japonica Group 5829
-
2.7.4.8 cytosol
-
 Saccharomyces cerevisiae 5829
-
2.7.4.8 additional information
-
 Bacillus subtilis
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.4.8 Mg2+ required Arabidopsis thaliana
2.7.4.8 Mg2+ required Bacillus subtilis
2.7.4.8 Mg2+ required Escherichia coli
2.7.4.8 Mg2+ required Lathyrus oleraceus
2.7.4.8 Mg2+ required Oryza sativa Japonica Group
2.7.4.8 Mg2+ required Saccharomyces cerevisiae
2.7.4.8 Mg2+ required Synechococcus elongatus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.4.8 ATP + GMP Escherichia coli
-
 ADP + GDP
-
 ?
2.7.4.8 ATP + GMP Synechococcus elongatus
-
 ADP + GDP
-
 ?
2.7.4.8 ATP + GMP Lathyrus oleraceus
-
 ADP + GDP
-
 ?
2.7.4.8 ATP + GMP Oryza sativa Japonica Group
-
 ADP + GDP
-
 ?
2.7.4.8 ATP + GMP Saccharomyces cerevisiae
-
 ADP + GDP
-
 ?
2.7.4.8 ATP + GMP Arabidopsis thaliana
-
 ADP + GDP
-
 ?
2.7.4.8 ATP + GMP Bacillus subtilis
-
 ADP + GDP
-
 ?
2.7.4.8 ATP + GMP Synechococcus elongatus PCC 7942
-
 ADP + GDP
-
 ?
2.7.4.8 ATP + GMP Oryza sativa Japonica Group Nipponbare
-
 ADP + GDP
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.8 Arabidopsis thaliana Q94JM2
-
-
2.7.4.8 Bacillus subtilis
-
-
-
2.7.4.8 Escherichia coli
-
-
-
2.7.4.8 Lathyrus oleraceus W8VZ39 cv. Toyonari, gene PsGKc
-
2.7.4.8 Lathyrus oleraceus W8VNI6 cv. Toyonari, gene PsGKpm
-
2.7.4.8 Oryza sativa Japonica Group Q2QPW1
-
-
2.7.4.8 Oryza sativa Japonica Group Q10M74
-
-
2.7.4.8 Oryza sativa Japonica Group Nipponbare Q2QPW1
-
-
2.7.4.8 Oryza sativa Japonica Group Nipponbare Q10M74
-
-
2.7.4.8 Saccharomyces cerevisiae P15454
-
-
2.7.4.8 Synechococcus elongatus
-
-
-
2.7.4.8 Synechococcus elongatus PCC 7942
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.4.8 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography Arabidopsis thaliana
2.7.4.8 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography Bacillus subtilis
2.7.4.8 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography Escherichia coli
2.7.4.8 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography Lathyrus oleraceus
2.7.4.8 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography Oryza sativa Japonica Group
2.7.4.8 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography Saccharomyces cerevisiae
2.7.4.8 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography Synechococcus elongatus
2.7.4.8 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography, native enzyme from chloroplasts by gel filtration Lathyrus oleraceus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.4.8 leaf
-
 Lathyrus oleraceus
-
2.7.4.8 leaf
-
 Oryza sativa Japonica Group
-
2.7.4.8 leaf
-
 Arabidopsis thaliana
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.8 ATP + GMP
-
 Escherichia coli ADP + GDP
-
 ?
2.7.4.8 ATP + GMP
-
 Synechococcus elongatus ADP + GDP
-
 ?
2.7.4.8 ATP + GMP
-
 Lathyrus oleraceus ADP + GDP
-
 ?
2.7.4.8 ATP + GMP
-
 Oryza sativa Japonica Group ADP + GDP
-
 ?
2.7.4.8 ATP + GMP
-
 Saccharomyces cerevisiae ADP + GDP
-
 ?
2.7.4.8 ATP + GMP
-
 Arabidopsis thaliana ADP + GDP
-
 ?
2.7.4.8 ATP + GMP
-
 Bacillus subtilis ADP + GDP
-
 ?
2.7.4.8 ATP + GMP
-
 Synechococcus elongatus PCC 7942 ADP + GDP
-
 ?
2.7.4.8 ATP + GMP
-
 Oryza sativa Japonica Group Nipponbare ADP + GDP
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.4.8 GK3
-
 Arabidopsis thaliana
2.7.4.8 GKc
-
 Lathyrus oleraceus
2.7.4.8 GKpm
-
 Oryza sativa Japonica Group
2.7.4.8 GKpm
-
 Arabidopsis thaliana
2.7.4.8 GKpm
-
 Lathyrus oleraceus
2.7.4.8 GMK3
-
 Arabidopsis thaliana
2.7.4.8 organellar GK
-
 Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.4.8 30
-
 assay at Arabidopsis thaliana
2.7.4.8 30
-
 assay at Bacillus subtilis
2.7.4.8 30
-
 assay at Escherichia coli
2.7.4.8 30
-
 assay at Lathyrus oleraceus
2.7.4.8 30
-
 assay at Oryza sativa Japonica Group
2.7.4.8 30
-
 assay at Saccharomyces cerevisiae
2.7.4.8 30
-
 assay at Synechococcus elongatus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.4.8 23
-
 GMP recombinant chloroplast isozyme, pH 7.5, 30°C Oryza sativa Japonica Group
2.7.4.8 52
-
 GMP recombinant isozyme, pH 7.5, 30°C Bacillus subtilis
2.7.4.8 70
-
 GMP recombinant cytosolic isozyme, pH 7.5, 30°C Oryza sativa Japonica Group
2.7.4.8 209
-
 GMP recombinant cytosolic isozyme, pH 7.5, 30°C Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.4.8 7.5
-
 assay at Escherichia coli
2.7.4.8 7.5
-
 assay at Synechococcus elongatus
2.7.4.8 7.5
-
 assay at Lathyrus oleraceus
2.7.4.8 7.5
-
 assay at Oryza sativa Japonica Group
2.7.4.8 7.5
-
 assay at Saccharomyces cerevisiae
2.7.4.8 7.5
-
 assay at Arabidopsis thaliana
2.7.4.8 7.5
-
 assay at Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.4.8 ATP
-
 Escherichia coli
2.7.4.8 ATP
-
 Synechococcus elongatus
2.7.4.8 ATP
-
 Lathyrus oleraceus
2.7.4.8 ATP
-
 Oryza sativa Japonica Group
2.7.4.8 ATP
-
 Saccharomyces cerevisiae
2.7.4.8 ATP
-
 Arabidopsis thaliana
2.7.4.8 ATP
-
 Bacillus subtilis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.4.8 0.0028
-
 guanosine 3',5'-bisdiphosphate versus GMP, pH 7.5, 30°C Oryza sativa Japonica Group

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.7.4.8 0.01
-
 versus GMP, pH 7.5, 30°C Oryza sativa Japonica Group guanosine 3',5'-bisdiphosphate

General Information

EC Number General Information Comment Organism
2.7.4.8 metabolism guanylate kinase is a key enzyme in guanine nucleotide biosynthesis, purine biosynthetic pathways in plant cells and bacteria, overview. Accumulation of guanosine 3',5'-bisdiphosphate has little effect on the guanine nucleotide profile of Escherichia coli Escherichia coli
2.7.4.8 metabolism guanylate kinase is a key enzyme in guanine nucleotide biosynthesis, purine biosynthetic pathways in plant cells and bacteria, overview Synechococcus elongatus
2.7.4.8 metabolism guanylate kinase is a key enzyme in guanine nucleotide biosynthesis, purine biosynthetic pathways in plant cells and bacteria, overview Lathyrus oleraceus
2.7.4.8 metabolism guanylate kinase is a key enzyme in guanine nucleotide biosynthesis, purine biosynthetic pathways in plant cells and bacteria, overview Oryza sativa Japonica Group
2.7.4.8 metabolism guanylate kinase is a key enzyme in guanine nucleotide biosynthesis, purine biosynthetic pathways in plant cells and bacteria, overview Saccharomyces cerevisiae
2.7.4.8 metabolism guanylate kinase is a key enzyme in guanine nucleotide biosynthesis, purine biosynthetic pathways in plant cells and bacteria, overview Arabidopsis thaliana
2.7.4.8 metabolism guanylate kinase is a key enzyme in guanine nucleotide biosynthesis, purine biosynthetic pathways in plant cells and bacteria, overview Bacillus subtilis
2.7.4.8 physiological function guanylate kinase is a key enzyme in guanine nucleotide biosynthesis that catalyzes the conversion of GMP to GDP, is a target of regulation by guanosine 3',5'-bisdiphosphate in chloroplasts. Plants have two distinct types of GK that are localized to organelles (GKpm) or to the cytosol (GKc) and both are essential for growth and development Lathyrus oleraceus
2.7.4.8 physiological function guanylate kinase is a key enzyme in guanine nucleotide biosynthesis that catalyzes the conversion of GMP to GDP, is a target of regulation by guanosine 3',5'-bisdiphosphate in chloroplasts. Plants have two distinct types of GK that are localized to organelles (GKpm) or to the cytosol (GKc) and both are essential for growth and development. guanosine 3',5'-bisdiphosphate plays a pivotal role in the regulation of GTP biosynthesis in chloroplasts through specific inhibition ofGKpmactivity, with the regulation of GTP biosynthesis in chloroplasts thus being independent of that in the cytosol Oryza sativa Japonica Group
2.7.4.8 physiological function guanylate kinase is a key enzyme in guanine nucleotide biosynthesis that catalyzes the conversion of GMP to GDP, is a target of regulation by guanosine 3',5'-bisdiphosphate in chloroplasts. Plants have two distinct types of GK that are localized to organelles (GKpm) or to the cytosol (GKc) and both are essential for growth and development. guanosine 3',5'-bisdiphosphate plays a pivotal role in the regulation of GTP biosynthesis in chloroplasts through specific inhibition ofGKpmactivity, with the regulation of GTP biosynthesis in chloroplasts thus being independent of that in the cytosol Arabidopsis thaliana
2.7.4.8 physiological function guanylate kinase is a key enzyme in guanine nucleotide biosynthesis that catalyzes the conversion of GMP to GDP, is a target of regulation by guanosine 3',5'-bisdiphosphate in chloroplasts. Plants have two distinct types of GK that are localized to organelles (GKpm) or to the cytosol (GKc) and both are essential for growth and development. guanosine 3',5'-bisdiphosphate plays a pivotal role in the regulation of GTP biosynthesis in chloroplasts through specific inhibition of GKpm activity, with the regulation of GTP biosynthesis in chloroplasts thus being independent of that in the cytosol Lathyrus oleraceus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.7.4.8 314
-
 GMP recombinant isozyme, pH 7.5, 30°C Bacillus subtilis
2.7.4.8 317
-
 GMP recombinant chloroplast isozyme, pH 7.5, 30°C Oryza sativa Japonica Group
2.7.4.8 344
-
 GMP recombinant cytosolic isozyme, pH 7.5, 30°C Oryza sativa Japonica Group
2.7.4.8 1347
-
 GMP recombinant cytosolic isozyme, pH 7.5, 30°C Escherichia coli