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Literature summary for 2.7.1.147 extracted from
- ADP-dependent phosphofructokinases from the archaeal order Methanosarcinales display redundant glucokinase activity (2017), Arch. Biochem. Biophys., 633, 85-92 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Methanococcoides burtonii |
| expression in Escherichia coli | Methanohalobium evestigatum |
| gene pfkC, phylogenetic analysis, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strains BL21(DE3) and BL21-C41(DE3) | Methanococcoides burtonii |
| gene pfkC, phylogenetic analysis, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strains BL21(DE3) and BL21-C41(DE3) | Methanohalobium evestigatum |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| ADP | - |
Methanococcoides burtonii |  |
| ADP | - |
Methanohalobium evestigatum | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.2 | - |
D-glucose | pH 7.8, 25°C | Methanococcoides burtonii | |
| 0.25 | - |
D-glucose | pH 7.8, 40°C | Methanohalobium evestigatum | |
| 0.64 | - |
ADP | pH 7.8, 25°C | Methanococcoides burtonii | |
| 1.5 | - |
ADP | pH 7.8, 40°C | Methanohalobium evestigatum | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | activates to less than 50% activity compared to Mg2+ activation | Methanococcoides burtonii | |
| Co2+ | activates to less than 50% activity compared to Mg2+ activation | Methanohalobium evestigatum | |
| Co2+ | the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+ | Methanococcoides burtonii | |
| Co2+ | the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+ | Methanohalobium evestigatum | |
| Mg2+ | required, activates, preferred divalent cation | Methanococcoides burtonii | |
| Mg2+ | required, activates, preferred divalent cation | Methanohalobium evestigatum | |
| Mg2+ | the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+ | Methanococcoides burtonii | |
| Mg2+ | the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+ | Methanohalobium evestigatum | |
| Mn2+ | activates to less than 50% activity compared to Mg2+ activation | Methanococcoides burtonii | |
| Mn2+ | activates to less than 50% activity compared to Mg2+ activation | Methanohalobium evestigatum | |
| Mn2+ | the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+ | Methanococcoides burtonii | |
| Mn2+ | the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+ | Methanohalobium evestigatum | |
| additional information | poor activation by Ca2+ probably due to steric hindrance | Methanococcoides burtonii | |
| additional information | poor activation by Ca2+ probably due to steric hindrance | Methanohalobium evestigatum | |
| Ni2+ | activates to less than 50% activity compared to Mg2+ activation | Methanococcoides burtonii | |
| Ni2+ | activates to less than 50% activity compared to Mg2+ activation | Methanohalobium evestigatum | |
| Ni2+ | the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+ | Methanococcoides burtonii | |
| Ni2+ | the enzyme shows phosphofructokinase and glucokinase activity in the presence of Mg2+, Co2+, Ni2+ and to a lesser extent Mn2+. In the case of glucokinase neither divalent metal cation reaches 50% of the activity obtained in the presence of Mg2+ | Methanohalobium evestigatum | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ADP + D-glucose | Methanococcoides burtonii | - |
AMP + D-glucose 6-phosphate | - |
? | |
| ADP + D-glucose | Methanohalobium evestigatum | - |
AMP + D-glucose 6-phosphate | - |
? | |
| ADP + D-glucose | Methanococcoides burtonii OCM 468 | - |
AMP + D-glucose 6-phosphate | - |
? | |
| ADP + D-glucose | Methanococcoides burtonii ACE-M | - |
AMP + D-glucose 6-phosphate | - |
? | |
| ADP + D-glucose | Methanococcoides burtonii NBRC 107633 | - |
AMP + D-glucose 6-phosphate | - |
? | |
| ADP + D-glucose | Methanohalobium evestigatum DSM 3721 | - |
AMP + D-glucose 6-phosphate | - |
? | |
| ADP + D-glucose | Methanohalobium evestigatum OCM 161 | - |
AMP + D-glucose 6-phosphate | - |
? | |
| ADP + D-glucose | Methanohalobium evestigatum Z-7303 | - |
AMP + D-glucose 6-phosphate | - |
? | |
| ADP + D-glucose | Methanohalobium evestigatum ATCC BAA-1072 | - |
AMP + D-glucose 6-phosphate | - |
? | |
| ADP + D-glucose | Methanohalobium evestigatum NBRC 107634 | - |
AMP + D-glucose 6-phosphate | - |
? | |
| ADP + D-glucose | Methanococcoides burtonii DSM 6242 | - |
AMP + D-glucose 6-phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanococcoides burtonii | Q12WB9 | bifunctional glucokinase/phosphofructokinase | - |
| Methanococcoides burtonii | Q12WB9 | cf. EC 2.7.1.146 | - |
| Methanococcoides burtonii ACE-M | Q12WB9 | cf. EC 2.7.1.146 | - |
| Methanococcoides burtonii DSM 6242 | Q12WB9 | bifunctional glucokinase/phosphofructokinase | - |
| Methanococcoides burtonii DSM 6242 | Q12WB9 | cf. EC 2.7.1.146 | - |
| Methanococcoides burtonii NBRC 107633 | Q12WB9 | cf. EC 2.7.1.146 | - |
| Methanococcoides burtonii OCM 468 | Q12WB9 | cf. EC 2.7.1.146 | - |
| Methanohalobium evestigatum | D7E8P3 | bifunctional glucokinase/phosphofructokinase | - |
| Methanohalobium evestigatum | D7E8P3 | cf. EC 2.7.1.146 | - |
| Methanohalobium evestigatum ATCC BAA-1072 | D7E8P3 | cf. EC 2.7.1.146 | - |
| Methanohalobium evestigatum DSM 3721 | D7E8P3 | cf. EC 2.7.1.146 | - |
| Methanohalobium evestigatum NBRC 107634 | D7E8P3 | cf. EC 2.7.1.146 | - |
| Methanohalobium evestigatum OCM 161 | D7E8P3 | cf. EC 2.7.1.146 | - |
| Methanohalobium evestigatum Z-7303 | D7E8P3 | cf. EC 2.7.1.146 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Methanococcoides burtonii |
- |
Methanohalobium evestigatum |
| recombinant N-terminally His6-tagged enzyme from Escherichia coli strains BL21(DE3) and BL21-C41(DE3) by heat treatment at 50°C for 30 min, nickel affinity chromatography, dialysis, and anion exchange chromatography | Methanohalobium evestigatum |
| recombinant N-terminally His6-tagged enzyme from Escherichia coli strains BL21(DE3) and BL21-C41(DE3) by nickel affinity chromatography, and dialysis | Methanococcoides burtonii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ADP + D-glucose | - |
Methanococcoides burtonii | AMP + D-glucose 6-phosphate | - |
? | |
| ADP + D-glucose | - |
Methanohalobium evestigatum | AMP + D-glucose 6-phosphate | - |
? | |
| ADP + D-glucose | - |
Methanococcoides burtonii OCM 468 | AMP + D-glucose 6-phosphate | - |
? | |
| ADP + D-glucose | - |
Methanococcoides burtonii ACE-M | AMP + D-glucose 6-phosphate | - |
? | |
| ADP + D-glucose | - |
Methanococcoides burtonii NBRC 107633 | AMP + D-glucose 6-phosphate | - |
? | |
| ADP + D-glucose | - |
Methanohalobium evestigatum DSM 3721 | AMP + D-glucose 6-phosphate | - |
? | |
| ADP + D-glucose | - |
Methanohalobium evestigatum OCM 161 | AMP + D-glucose 6-phosphate | - |
? | |
| ADP + D-glucose | - |
Methanohalobium evestigatum Z-7303 | AMP + D-glucose 6-phosphate | - |
? | |
| ADP + D-glucose | - |
Methanohalobium evestigatum ATCC BAA-1072 | AMP + D-glucose 6-phosphate | - |
? | |
| ADP + D-glucose | - |
Methanohalobium evestigatum NBRC 107634 | AMP + D-glucose 6-phosphate | - |
? | |
| ADP + D-glucose | - |
Methanococcoides burtonii DSM 6242 | AMP + D-glucose 6-phosphate | - |
? | |
| additional information | the enzyme from Methanococcoides burtonii also shows glucokinase activity, a bifunctional PFK/GK enzyme. Methanococcoides burtonii has a truncate glucokinase gene with a large deletion at the C-terminus, where the catalytic GXGD motif is located, but it is able to show glucokinase activity. Substrate specificity analysis, structure-function analysis | Methanococcoides burtonii | ? | - |
- |
|
| additional information | the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional PFK/GK enzyme | Methanohalobium evestigatum | ? | - |
- |
|
| additional information | the enzyme from Methanococcoides burtonii also shows glucokinase activity, a bifunctional PFK/GK enzyme. Methanococcoides burtonii has a truncate glucokinase gene with a large deletion at the C-terminus, where the catalytic GXGD motif is located, but it is able to show glucokinase activity. Substrate specificity analysis, structure-function analysis | Methanococcoides burtonii OCM 468 | ? | - |
- |
|
| additional information | the enzyme from Methanococcoides burtonii also shows glucokinase activity, a bifunctional PFK/GK enzyme. Methanococcoides burtonii has a truncate glucokinase gene with a large deletion at the C-terminus, where the catalytic GXGD motif is located, but it is able to show glucokinase activity. Substrate specificity analysis, structure-function analysis | Methanococcoides burtonii ACE-M | ? | - |
- |
|
| additional information | the enzyme from Methanococcoides burtonii also shows glucokinase activity, a bifunctional PFK/GK enzyme. Methanococcoides burtonii has a truncate glucokinase gene with a large deletion at the C-terminus, where the catalytic GXGD motif is located, but it is able to show glucokinase activity. Substrate specificity analysis, structure-function analysis | Methanococcoides burtonii NBRC 107633 | ? | - |
- |
|
| additional information | the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional PFK/GK enzyme | Methanohalobium evestigatum DSM 3721 | ? | - |
- |
|
| additional information | the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional PFK/GK enzyme | Methanohalobium evestigatum OCM 161 | ? | - |
- |
|
| additional information | the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional PFK/GK enzyme | Methanohalobium evestigatum Z-7303 | ? | - |
- |
|
| additional information | the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional PFK/GK enzyme | Methanohalobium evestigatum ATCC BAA-1072 | ? | - |
- |
|
| additional information | the enzyme from Methanohalobium evestigatum also shows phosphofructokinase activity, a bifunctional PFK/GK enzyme | Methanohalobium evestigatum NBRC 107634 | ? | - |
- |
|
| additional information | the enzyme from Methanococcoides burtonii also shows glucokinase activity, a bifunctional PFK/GK enzyme. Methanococcoides burtonii has a truncate glucokinase gene with a large deletion at the C-terminus, where the catalytic GXGD motif is located, but it is able to show glucokinase activity. Substrate specificity analysis, structure-function analysis | Methanococcoides burtonii DSM 6242 | ? | - |
- |
|
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ADP-dependent glucokinase | - |
Methanococcoides burtonii |
| ADP-dependent glucokinase | - |
Methanohalobium evestigatum |
| ADP-Pfk | - |
Methanococcoides burtonii |
| ADP-Pfk | - |
Methanohalobium evestigatum |
| More | see also EC 2.7.1.146 | Methanococcoides burtonii |
| More | see also EC 2.7.1.146 | Methanohalobium evestigatum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Methanococcoides burtonii |
| 40 | - |
assay at | Methanohalobium evestigatum |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.8 | - |
ADP | pH 7.8, 25°C | Methanococcoides burtonii | |
| 2 | - |
ADP | pH 7.8, 40°C | Methanohalobium evestigatum | |
| 14 | - |
D-glucose | pH 7.8, 25°C | Methanococcoides burtonii | |
| 16 | - |
D-glucose | pH 7.8, 40°C | Methanohalobium evestigatum | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.8 | - |
assay at | Methanococcoides burtonii |
| 7.8 | - |
assay at | Methanohalobium evestigatum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ADP | - |
Methanococcoides burtonii | |
| ADP | - |
Methanohalobium evestigatum | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 3 | - |
ADP | pH 7.8, 40°C | Methanohalobium evestigatum | |
| 4 | - |
ADP | pH 7.8, 25°C | Methanococcoides burtonii | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | kinetic analyses of the phosphofructokinase annotated enzyme from Methanococcoides burtonii demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities | Methanococcoides burtonii |
| evolution | kinetic analyses of the phosphofructokinase annotated enzyme from, Methanohalobium evestigatum demonstrate that this enzyme is bifunctional. The high conservation of the active site residues of all the enzymes from the order Methanosarcinales suggest that they should be bifunctional, as is reported for the ADP-dependent kinases from Methanococcales, highlighting the redundancy of the glucokinase activity in this archaeal group. In Methanosarcinales two genes have been described. One of them corresponds to a theoretically functional GK enzyme since it presents the GXGD and NXXE catalytic motifs. PFKs from Methanosarcinales should be bifunctional with PFK and GK activities | Methanohalobium evestigatum |
| additional information | enzyme structure and homology modeling | Methanohalobium evestigatum |
| additional information | enzyme structure and homology modeling. Identification of three motifs responsible for sugar substrate specificity in the ADP-dependent kinases family not described previously. According to the sequence number of the annotated ADP-dependent PFK from Methanococcoides burtonii, these motifs are: motif 1: 86G-X-(P/A/G)-X-(E/A)90, motif 2: 179(I/V)-(N/H)180-X-(I/V)-X-(E/D)184 and motif 3: 205R-X-I-X-X-X-(R/D)211 | Methanococcoides burtonii |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.3 | - |
ADP | pH 7.8, 40°C | Methanohalobium evestigatum | |
| 11 | - |
ADP | pH 7.8, 25°C | Methanococcoides burtonii | |
| 41 | - |
D-glucose | pH 7.8, 25°C | Methanococcoides burtonii | |
| 63 | - |
D-glucose | pH 7.8, 40°C | Methanohalobium evestigatum | |
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