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Literature summary extracted from

  • Currie, M.A.; Merino, F.; Skarina, T.; Wong, A.H.; Singer, A.; Brown, G.; Savchenko, A.; Caniuguir, A.; Guixe, V.; Yakunin, A.F.; Jia, Z.
    ADP-dependent 6-phosphofructokinase from Pyrococcus horikoshii OT3: structure determination and biochemical characterization of PH1645 (2009), J. Biol. Chem., 284, 22664-22671.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.146 expressed in Escherichia coli BL21(DE3) and DL41(DE3) cells Pyrococcus horikoshii
2.7.1.146 recombinant wild type and mutant native and selenomethionine-labeled proteins are expressed in BL21(DE3) and DL41(DE3) Escherichia coli cells Pyrococcus horikoshii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.146 hanging drop vapor diffusion method, the apo-enzyme is crystallized using 22% PEG 4000, 0.1 M Tris-HCl, pH 8.5, and 0.2 M LiSO4, at 21°C. Crystals of the PFK complex with AMP are obtained by crystallization of the PFK D17A protein in the presence of 20% PEG 3350, 0.2 M lithium citrate, 10 mM D-fructose 6-phosphate, and 5 mM ADP Pyrococcus horikoshii
2.7.1.146 through hanging drop vapor diffusion at 21°C by mixing protein solution with solution consisting of 22% PEG 4000, 0.1 M Tris-HCl, pH 8.5, and 0.2 M Li2SO4, crystals of the ADP-dependent 6-phosphofructokinase complex with AMP are obtained by crystallization of the mutant protein D17A protein in the presence of 20% PEG 3350, 0.2 M lithium citrate, 10 mM fructose 6-phosphate, and 5 mM ADPcrystal structure of ADP-dependent 6-phosphofructokinase in both apo- and AMP-bound forms determined to 2.0 A and 1.9 A resolution Pyrococcus horikoshii

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.146 A71E production by site-directed mutagenesis Pyrococcus horikoshii
2.7.1.146 A71E the mutant shows slightly decreased kcat compared to the wild type enzyme Pyrococcus horikoshii
2.7.1.146 D17A production by site-directed mutagenesis Pyrococcus horikoshii
2.7.1.146 D17A the mutant shows severely decreased kcat compared to the wild type enzyme Pyrococcus horikoshii
2.7.1.146 D433A production by site-directed mutagenesis, loss of PFK activity Pyrococcus horikoshii
2.7.1.146 D433A the mutant shows no acitivity Pyrococcus horikoshii
2.7.1.146 K158A production by site-directed mutagenesis Pyrococcus horikoshii
2.7.1.146 K158A the mutant shows slightly decreased kcat compared to the wild type enzyme Pyrococcus horikoshii
2.7.1.146 N15A production by site-directed mutagenesis Pyrococcus horikoshii
2.7.1.146 N15A the mutant shows increased kcat compared to the wild type enzyme Pyrococcus horikoshii
2.7.1.146 N160A production by site-directed mutagenesis Pyrococcus horikoshii
2.7.1.146 N160A the mutant shows strongly increased kcat compared to the wild type enzyme Pyrococcus horikoshii
2.7.1.146 Q224A production by site-directed mutagenesis Pyrococcus horikoshii
2.7.1.146 Q224A the mutant shows increased kcat compared to the wild type enzyme Pyrococcus horikoshii
2.7.1.146 Q97A production by site-directed mutagenesis Pyrococcus horikoshii
2.7.1.146 Q97A the mutant shows decreased kcat compared to the wild type enzyme Pyrococcus horikoshii
2.7.1.146 R185A production by site-directed mutagenesis Pyrococcus horikoshii
2.7.1.146 R185A the mutant shows no acitivity Pyrococcus horikoshii
2.7.1.146 R191A production by site-directed mutagenesis Pyrococcus horikoshii
2.7.1.146 R191A the mutant shows decreased kcat compared to the wild type enzyme Pyrococcus horikoshii
2.7.1.146 R191E production by site-directed mutagenesis Pyrococcus horikoshii
2.7.1.146 R191E the mutant shows almost wild type enzyme activity Pyrococcus horikoshii
2.7.1.146 S183A the mutant shows strongly increased kcat compared to the wild type enzyme Pyrococcus horikoshii
2.7.1.146 S183E production by site-directed mutagenesis, the S183E mutant displays significantly less activity when the phosphoryl donor is replaced with IDP, UDP, GDP, or CDP compared with the wild type Pyrococcus horikoshii
2.7.1.146 S183E the mutant displays significantly less activity when the phosphoryl donor ADP is replaced with IDP, UDP, GDP, or CDP, compared with the wild type Pyrococcus horikoshii
2.7.1.146 S189A production by site-directed mutagenesis Pyrococcus horikoshii
2.7.1.146 S189A the mutant shows decreased kcat compared to the wild type enzyme Pyrococcus horikoshii
2.7.1.146 S263A production by site-directed mutagenesis Pyrococcus horikoshii
2.7.1.146 S263A the mutant shows increased kcat compared to the wild type enzyme Pyrococcus horikoshii

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.146 Ca2+ about 50% activity at 2.5 mM Pyrococcus horikoshii
2.7.1.146 Mg2+ about 60% activity at 2.5 mM Pyrococcus horikoshii
2.7.1.146 Mn2+ about 70% activity at 2.5 mM Pyrococcus horikoshii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.146 0.00395
-
 D-fructose 6-phosphate A71E mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.00395
-
 D-fructose 6-phosphate mutant enzyme A71E, at 50°C Pyrococcus horikoshii
2.7.1.146 0.00708
-
 D-fructose 6-phosphate Q97A mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.00708
-
 D-fructose 6-phosphate mutant enzyme Q97A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.00747
-
 ADP Q97A mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.00747
-
 ADP mutant enzyme Q97A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.00902
-
 D-fructose 6-phosphate S189A mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.00902
-
 D-fructose 6-phosphate mutant enzyme S189A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0127
-
 D-fructose 6-phosphate D433A mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0127
-
 D-fructose 6-phosphate mutant enzyme D433A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0132
-
 ADP wild type enzyme, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0136
-
 ADP A71E mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0136
-
 ADP mutant enzyme A71E, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0139
-
 ADP D433A mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0139
-
 ADP mutant enzyme D433A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0145
-
 ADP R191A mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0145
-
 ADP mutant enzyme R191A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0152
-
 D-fructose 6-phosphate wild type enzyme, at 50°C Pyrococcus horikoshii
2.7.1.146 0.016
-
 ADP S189A mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.016
-
 ADP mutant enzyme S189A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0208
-
 ADP S263A mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0208
-
 ADP mutant enzyme S263A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0238
-
 ADP N15A mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0238
-
 ADP mutant enzyme N15A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0295
-
 ADP Q224A mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0295
-
 ADP mutant enzyme Q224A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0296
-
 ADP S183E mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0296
-
 ADP mutant enzyme S183E, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0379
-
 ADP K158A mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0379
-
 ADP mutant enzyme K158A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0386
-
 D-fructose 6-phosphate Q224A mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0386
-
 D-fructose 6-phosphate mutant enzyme Q224A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0395
-
 D-fructose 6-phosphate S263A mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0395
-
 D-fructose 6-phosphate mutant enzyme S263A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0605
-
 ADP R191E mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0605
-
 ADP mutant enzyme R191E, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0724
-
 ADP N160A mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0724
-
 ADP mutant enzyme N160A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0865
-
 D-fructose 6-phosphate S183E mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.0865
-
 D-fructose 6-phosphate mutant enzyme S183E, at 50°C Pyrococcus horikoshii
2.7.1.146 0.103
-
 D-fructose 6-phosphate N15A mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.103
-
 D-fructose 6-phosphate mutant enzyme N15A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.2544
-
 D-fructose 6-phosphate R191A mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.2544
-
 D-fructose 6-phosphate mutant enzyme R191A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.318
-
 D-fructose 6-phosphate R185A mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.318
-
 D-fructose 6-phosphate mutant enzyme R185A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.415
-
 D-fructose 6-phosphate N160A mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.415
-
 D-fructose 6-phosphate mutant enzyme N160A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.473
-
 ADP R185A mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 0.473
-
 ADP mutant enzyme R185A, at 50°C Pyrococcus horikoshii
2.7.1.146 4.87
-
 D-fructose 6-phosphate R191E mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 4.87
-
 D-fructose 6-phosphate mutant enzyme R191E, at 50°C Pyrococcus horikoshii
2.7.1.146 6.5
-
 D-fructose 6-phosphate K158A mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 22.6
-
 D-fructose 6-phosphate D17A mutant, at 50°C Pyrococcus horikoshii
2.7.1.146 22.6
-
 D-fructose 6-phosphate mutant enzyme D17A, at 50°C Pyrococcus horikoshii
2.7.1.146 65
-
 D-fructose 6-phosphate mutant enzyme K158A, at 50°C Pyrococcus horikoshii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.146 CaCl2 2 mM ADP and 2 mM D-fructose 6-phosphate, CaCl2 show the lowest activity with 75% of the activity measured in the presence of MgCl2, activity does not change with the cation concentration in the range of 2.5 to 7 mM Pyrococcus horikoshii
2.7.1.146 MgSO4 2 mM ADP and 2 mM D-fructose 6-phosphate, magnesium is tested with 2 counter ions to discard any effect of the anion Pyrococcus horikoshii
2.7.1.146 MnCl2 2 mM ADP and 2 mM D-fructose 6-phosphate, increase in enzyme activity with the increase in MnCl2 concentration from 2.5 to 7 mM is observed Pyrococcus horikoshii
2.7.1.146 additional information no significant activity is detected in the presence of Zn2+ Pyrococcus horikoshii
2.7.1.146 Ni2+ highest activity in the presence of 2.5 mM NiSO4 Pyrococcus horikoshii
2.7.1.146 NiSO4 2 mM ADP and 2 mM D-fructose 6-phosphate, highest PhPFK activity is obtained with NiSO4 (97 units/mg), decrease in enzyme activity with the increase in MnCl2 concentration from 2.5 to 7 mM is observed Pyrococcus horikoshii
2.7.1.146 ZnCl2 2 mM ADP and 2 mM D-fructose 6-phosphate, no significant activity Pyrococcus horikoshii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.146 ADP + D-fructose 6-phosphate Pyrococcus horikoshii
-
 AMP + D-fructose 1,6-bisphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.146 Pyrococcus horikoshii
-
-
-
2.7.1.146 Pyrococcus horikoshii O59355 strain OT3
-
2.7.1.146 Pyrococcus horikoshii OT-3 O59355 strain OT3
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.146 by using nickel-nitrilotriacetic acid affinity chromatography and gel filtration Pyrococcus horikoshii
2.7.1.146 Ni-NTA column chromatography Pyrococcus horikoshii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.146 ADP + D-fructose 6-phosphate
-
 Pyrococcus horikoshii AMP + D-fructose 1,6-bisphosphate
-
 ?
2.7.1.146 D-fructose 6-phosphate + ADP 100% activity Pyrococcus horikoshii D-fructose 1,6-bisphosphate + AMP
-
 ?
2.7.1.146 D-fructose 6-phosphate + ADP 100% activity Pyrococcus horikoshii OT-3 D-fructose 1,6-bisphosphate + AMP
-
 ?
2.7.1.146 D-fructose 6-phosphate + CDP about 35% activity compared to ADP Pyrococcus horikoshii D-fructose 1,6-bisphosphate + CMP
-
 ?
2.7.1.146 D-fructose 6-phosphate + CDP about 35% activity compared to ADP Pyrococcus horikoshii OT-3 D-fructose 1,6-bisphosphate + CMP
-
 ?
2.7.1.146 D-fructose 6-phosphate + GDP about 50% activity compared to ADP Pyrococcus horikoshii D-fructose 1,6-bisphosphate + GMP
-
 ?
2.7.1.146 D-fructose 6-phosphate + GDP about 50% activity compared to ADP Pyrococcus horikoshii OT-3 D-fructose 1,6-bisphosphate + GMP
-
 ?
2.7.1.146 D-fructose 6-phosphate + IDP about 50% activity compared to ADP Pyrococcus horikoshii D-fructose 1,6-bisphosphate + IMP
-
 ?
2.7.1.146 D-fructose 6-phosphate + IDP about 50% activity compared to ADP Pyrococcus horikoshii OT-3 D-fructose 1,6-bisphosphate + IMP
-
 ?
2.7.1.146 D-fructose 6-phosphate + UDP about 105% activity compared to ADP Pyrococcus horikoshii D-fructose 1,6-bisphosphate + UMP
-
 ?
2.7.1.146 D-fructose 6-phosphate + UDP about 105% activity compared to ADP Pyrococcus horikoshii OT-3 D-fructose 1,6-bisphosphate + UMP
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.1.146 ADP-dependent 6-phosphofructokinase
-
 Pyrococcus horikoshii
2.7.1.146 ADP-Pfk
-
 Pyrococcus horikoshii
2.7.1.146 PhPFK
-
 Pyrococcus horikoshii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.146 50
-
 assay at Pyrococcus horikoshii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.1.146 0.0048
-
 D-fructose 6-phosphate D433A mutant Pyrococcus horikoshii
2.7.1.146 0.0048
-
 D-fructose 6-phosphate mutant enzyme D433A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.31
-
 D-fructose 6-phosphate R185A mutant Pyrococcus horikoshii
2.7.1.146 0.351
-
 D-fructose 6-phosphate mutant enzyme R185A, at 50°C Pyrococcus horikoshii
2.7.1.146 1.98
-
 D-fructose 6-phosphate D17A mutant Pyrococcus horikoshii
2.7.1.146 1.98
-
 D-fructose 6-phosphate mutant enzyme D17A, at 50°C Pyrococcus horikoshii
2.7.1.146 13
-
 D-fructose 6-phosphate Q97A mutant Pyrococcus horikoshii
2.7.1.146 13
-
 D-fructose 6-phosphate mutant enzyme Q97A, at 50°C Pyrococcus horikoshii
2.7.1.146 25.5
-
 D-fructose 6-phosphate S189A mutant Pyrococcus horikoshii
2.7.1.146 25.5
-
 D-fructose 6-phosphate mutant enzyme S189A, at 50°C Pyrococcus horikoshii
2.7.1.146 27.4
-
 D-fructose 6-phosphate R191A mutant Pyrococcus horikoshii
2.7.1.146 27.4
-
 D-fructose 6-phosphate mutant enzyme R191A, at 50°C Pyrococcus horikoshii
2.7.1.146 39.3
-
 D-fructose 6-phosphate A71E mutant Pyrococcus horikoshii
2.7.1.146 39.3
-
 D-fructose 6-phosphate mutant enzyme A71E, at 50°C Pyrococcus horikoshii
2.7.1.146 41
-
 D-fructose 6-phosphate K158A mutant Pyrococcus horikoshii
2.7.1.146 41
-
 D-fructose 6-phosphate mutant enzyme K158A, at 50°C Pyrococcus horikoshii
2.7.1.146 42.5
-
 D-fructose 6-phosphate R191E mutant Pyrococcus horikoshii
2.7.1.146 42.5
-
 D-fructose 6-phosphate mutant enzyme R191E, at 50°C Pyrococcus horikoshii
2.7.1.146 45.5
-
 D-fructose 6-phosphate wild type enzyme, at 50°C Pyrococcus horikoshii
2.7.1.146 64.1
-
 D-fructose 6-phosphate S263A mutant Pyrococcus horikoshii
2.7.1.146 64.1
-
 D-fructose 6-phosphate mutant enzyme S263A, at 50°C Pyrococcus horikoshii
2.7.1.146 65.3
-
 D-fructose 6-phosphate Q224A mutant Pyrococcus horikoshii
2.7.1.146 65.3
-
 D-fructose 6-phosphate mutant enzyme Q224A, at 50°C Pyrococcus horikoshii
2.7.1.146 91.1
-
 D-fructose 6-phosphate N15A mutant Pyrococcus horikoshii
2.7.1.146 91.1
-
 D-fructose 6-phosphate mutant enzyme N15A, at 50°C Pyrococcus horikoshii
2.7.1.146 91.7
-
 D-fructose 6-phosphate S183E mutant Pyrococcus horikoshii
2.7.1.146 91.7
-
 D-fructose 6-phosphate mutant enzyme S183E, at 50°C Pyrococcus horikoshii
2.7.1.146 151
-
 D-fructose 6-phosphate N160A mutant Pyrococcus horikoshii
2.7.1.146 151
-
 D-fructose 6-phosphate mutant enzyme N160A, at 50°C Pyrococcus horikoshii

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.146 ADP
-
 Pyrococcus horikoshii
2.7.1.146 CDP
-
 Pyrococcus horikoshii
2.7.1.146 GDP
-
 Pyrococcus horikoshii
2.7.1.146 IDP
-
 Pyrococcus horikoshii
2.7.1.146 UDP
-
 Pyrococcus horikoshii

General Information

EC Number General Information Comment Organism
2.7.1.146 metabolism Embden-Meyerhof glycolytic pathway, early step Pyrococcus horikoshii

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.7.1.146 additional information
-
 ADP the calculated value for UDP is 40times higher than that of ADP, indicating a strong preference for ADP over UDP as the phosphoryl group donor Pyrococcus horikoshii
2.7.1.146 0.0876
-
 D-fructose 6-phosphate mutant enzyme D17A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.345
-
 ADP mutant enzyme D433A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.378
-
 D-fructose 6-phosphate mutant enzyme D433A, at 50°C Pyrococcus horikoshii
2.7.1.146 0.742
-
 ADP mutant enzyme R185A, at 50°C Pyrococcus horikoshii
2.7.1.146 1.1
-
 D-fructose 6-phosphate mutant enzyme R185A, at 50°C Pyrococcus horikoshii
2.7.1.146 6.31
-
 D-fructose 6-phosphate mutant enzyme K158A, at 50°C Pyrococcus horikoshii
2.7.1.146 8.73
-
 D-fructose 6-phosphate mutant enzyme R191E, at 50°C Pyrococcus horikoshii
2.7.1.146 107
-
 D-fructose 6-phosphate mutant enzyme R191A, at 50°C Pyrococcus horikoshii
2.7.1.146 364
-
 D-fructose 6-phosphate mutant enzyme N160A, at 50°C Pyrococcus horikoshii
2.7.1.146 702
-
 ADP mutant enzyme R191E, at 50°C Pyrococcus horikoshii
2.7.1.146 884
-
 D-fructose 6-phosphate mutant enzyme N15A, at 50°C Pyrococcus horikoshii
2.7.1.146 1060
-
 D-fructose 6-phosphate mutant enzyme S183E, at 50°C Pyrococcus horikoshii
2.7.1.146 1080
-
 ADP mutant enzyme K158A, at 50°C Pyrococcus horikoshii
2.7.1.146 1600
-
 ADP mutant enzyme S189A, at 50°C Pyrococcus horikoshii
2.7.1.146 1620
-
 D-fructose 6-phosphate mutant enzyme S263A, at 50°C Pyrococcus horikoshii
2.7.1.146 1690
-
 D-fructose 6-phosphate mutant enzyme Q224A, at 50°C Pyrococcus horikoshii
2.7.1.146 1720
-
 D-fructose 6-phosphate mutant enzyme A71E, at 50°C Pyrococcus horikoshii
2.7.1.146 1740
-
 ADP mutant enzyme Q97A, at 50°C Pyrococcus horikoshii
2.7.1.146 1840
-
 D-fructose 6-phosphate mutant enzyme Q97A, at 50°C Pyrococcus horikoshii
2.7.1.146 1890
-
 ADP mutant enzyme R191A, at 50°C Pyrococcus horikoshii
2.7.1.146 2090
-
 ADP mutant enzyme N160A, at 50°C Pyrococcus horikoshii
2.7.1.146 2210
-
 ADP mutant enzyme Q224A, at 50°C Pyrococcus horikoshii
2.7.1.146 2820
-
 ADP mutant enzyme A71E, at 50°C Pyrococcus horikoshii
2.7.1.146 2830
-
 D-fructose 6-phosphate mutant enzyme S189A, at 50°C Pyrococcus horikoshii
2.7.1.146 2990
-
 D-fructose 6-phosphate wild type enzyme, at 50°C Pyrococcus horikoshii
2.7.1.146 3080
-
 ADP mutant enzyme S263A, at 50°C Pyrococcus horikoshii
2.7.1.146 3100
-
 ADP mutant enzyme S183E, at 50°C Pyrococcus horikoshii
2.7.1.146 3450
-
 ADP wild type enzyme, at 50°C Pyrococcus horikoshii
2.7.1.146 3830
-
 ADP mutant enzyme N15A, at 50°C Pyrococcus horikoshii