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Literature summary for 2.7.1.146 extracted from

  • Zamora, R.; Gonzalez-Órdenes, F.; Castro-Fernández, V.; Guixé, V.
    ADP-dependent phosphofructokinases from the archaeal order Methanosarcinales display redundant glucokinase activity (2017), Arch. Biochem. Biophys., 633, 85-92 .
    View publication on PubMed
Search for more literature for 2.7.1.146

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 substrate inhibition Methanococcoides burtonii
ADP substrate inhibition Methanohalobium evestigatum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.023
-
 D-fructose 6-phosphate pH 7.8, 25°C Methanococcoides burtonii
0.034
-
 D-fructose 6-phosphate pH 7.8, 40°C Methanohalobium evestigatum
11
-
 ADP pH 7.8, 40°C Methanohalobium evestigatum
20
-
 ADP pH 7.8, 25°C Methanococcoides burtonii

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activates Methanococcoides burtonii
Co2+ activates 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 Methanococcoides burtonii
Mg2+ required, activates 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 slightly Methanococcoides burtonii
Mn2+ activates slightly 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 Methanococcoides burtonii
Ni2+ activates 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-fructose 6-phosphate Methanococcoides burtonii
-
 AMP + D-fructose 1,6-bisphosphate
-
 ?
ADP + D-fructose 6-phosphate Methanohalobium evestigatum
-
 AMP + D-fructose 1,6-bisphosphate
-
 ?
ADP + D-fructose 6-phosphate Methanococcoides burtonii OCM 468
-
 AMP + D-fructose 1,6-bisphosphate
-
 ?
ADP + D-fructose 6-phosphate Methanococcoides burtonii ACE-M
-
 AMP + D-fructose 1,6-bisphosphate
-
 ?
ADP + D-fructose 6-phosphate Methanococcoides burtonii NBRC 107633
-
 AMP + D-fructose 1,6-bisphosphate
-
 ?
ADP + D-fructose 6-phosphate Methanohalobium evestigatum DSM 3721
-
 AMP + D-fructose 1,6-bisphosphate
-
 ?
ADP + D-fructose 6-phosphate Methanohalobium evestigatum OCM 161
-
 AMP + D-fructose 1,6-bisphosphate
-
 ?
ADP + D-fructose 6-phosphate Methanohalobium evestigatum Z-7303
-
 AMP + D-fructose 1,6-bisphosphate
-
 ?
ADP + D-fructose 6-phosphate Methanohalobium evestigatum ATCC BAA-1072
-
 AMP + D-fructose 1,6-bisphosphate
-
 ?
ADP + D-fructose 6-phosphate Methanohalobium evestigatum NBRC 107634
-
 AMP + D-fructose 1,6-bisphosphate
-
 ?
ADP + D-fructose 6-phosphate Methanococcoides burtonii DSM 6242
-
 AMP + D-fructose 1,6-bisphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Methanococcoides burtonii Q12WB9
-
-
Methanococcoides burtonii Q12WB9 bifunctional glucokinase/phosphofructokinase
-
Methanococcoides burtonii ACE-M Q12WB9
-
-
Methanococcoides burtonii DSM 6242 Q12WB9
-
-
Methanococcoides burtonii DSM 6242 Q12WB9 bifunctional glucokinase/phosphofructokinase
-
Methanococcoides burtonii NBRC 107633 Q12WB9
-
-
Methanococcoides burtonii OCM 468 Q12WB9
-
-
Methanohalobium evestigatum D7E8P3
-
-
Methanohalobium evestigatum D7E8P3 bifunctional glucokinase/phosphofructokinase
-
Methanohalobium evestigatum ATCC BAA-1072 D7E8P3
-
-
Methanohalobium evestigatum DSM 3721 D7E8P3
-
-
Methanohalobium evestigatum DSM 3721 D7E8P3 bifunctional glucokinase/phosphofructokinase
-
Methanohalobium evestigatum NBRC 107634 D7E8P3
-
-
Methanohalobium evestigatum OCM 161 D7E8P3
-
-
Methanohalobium evestigatum Z-7303 D7E8P3
-
-

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-fructose 6-phosphate
-
 Methanococcoides burtonii AMP + D-fructose 1,6-bisphosphate
-
 ?
ADP + D-fructose 6-phosphate
-
 Methanohalobium evestigatum AMP + D-fructose 1,6-bisphosphate
-
 ?
ADP + D-fructose 6-phosphate
-
 Methanococcoides burtonii OCM 468 AMP + D-fructose 1,6-bisphosphate
-
 ?
ADP + D-fructose 6-phosphate
-
 Methanococcoides burtonii ACE-M AMP + D-fructose 1,6-bisphosphate
-
 ?
ADP + D-fructose 6-phosphate
-
 Methanococcoides burtonii NBRC 107633 AMP + D-fructose 1,6-bisphosphate
-
 ?
ADP + D-fructose 6-phosphate
-
 Methanohalobium evestigatum DSM 3721 AMP + D-fructose 1,6-bisphosphate
-
 ?
ADP + D-fructose 6-phosphate
-
 Methanohalobium evestigatum OCM 161 AMP + D-fructose 1,6-bisphosphate
-
 ?
ADP + D-fructose 6-phosphate
-
 Methanohalobium evestigatum Z-7303 AMP + D-fructose 1,6-bisphosphate
-
 ?
ADP + D-fructose 6-phosphate
-
 Methanohalobium evestigatum ATCC BAA-1072 AMP + D-fructose 1,6-bisphosphate
-
 ?
ADP + D-fructose 6-phosphate
-
 Methanohalobium evestigatum NBRC 107634 AMP + D-fructose 1,6-bisphosphate
-
 ?
ADP + D-fructose 6-phosphate
-
 Methanococcoides burtonii DSM 6242 AMP + D-fructose 1,6-bisphosphate
-
 ?
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-terminal, 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 glucokinase 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-terminal, 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-terminal, 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-terminal, 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 glucokinase activity, a bifunctional PFK/GK enzyme Methanohalobium evestigatum DSM 3721 ?
-
-
additional information the enzyme from Methanohalobium evestigatum also shows glucokinase activity, a bifunctional PFK/GK enzyme Methanohalobium evestigatum OCM 161 ?
-
-
additional information the enzyme from Methanohalobium evestigatum also shows glucokinase activity, a bifunctional PFK/GK enzyme Methanohalobium evestigatum Z-7303 ?
-
-
additional information the enzyme from Methanohalobium evestigatum also shows glucokinase activity, a bifunctional PFK/GK enzyme Methanohalobium evestigatum ATCC BAA-1072 ?
-
-
additional information the enzyme from Methanohalobium evestigatum also shows glucokinase 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-terminal, 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 phosphofructokinase
-
 Methanococcoides burtonii
ADP-dependent phosphofructokinase
-
 Methanohalobium evestigatum
ADP-Pfk
-
 Methanococcoides burtonii
ADP-Pfk
-
 Methanohalobium evestigatum
More see also EC 2.7.1.147 Methanococcoides burtonii
More see also EC 2.7.1.147 Methanohalobium evestigatum
PFK
-
 Methanococcoides burtonii
PFK
-
 Methanohalobium evestigatum
PFK-ADP
-
 Methanococcoides burtonii
PFK-ADP
-
 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
0.9
-
 ADP pH 7.8, 25°C Methanococcoides burtonii
1.9
-
 ADP pH 7.8, 40°C Methanohalobium evestigatum
8.9
-
 D-fructose 6-phosphate pH 7.8, 25°C Methanococcoides burtonii
9.5
-
 D-fructose 6-phosphate pH 7.8, 40°C Methanohalobium evestigatum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
 assay at Methanococcoides burtonii
6.5
-
 assay at Methanohalobium evestigatum
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. 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. 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
0.036
-
 ADP pH 7.8, 25°C Methanococcoides burtonii
0.18
-
 ADP pH 7.8, 40°C Methanohalobium evestigatum
280
-
 D-fructose 6-phosphate pH 7.8, 40°C Methanohalobium evestigatum
340
-
 D-fructose 6-phosphate pH 7.8, 25°C Methanococcoides burtonii