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discounted EARLY registration ends Dec 31, 2014
BioCyc websites MAYBE down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites MAYBE down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites MAYBE down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites MAYBE down
12/28 - 12/31
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MetaCyc Enzyme: ADP-dependent phosphofructokinase

Gene: pfkA Accession Number: G-9171 (MetaCyc)

Synonyms: pfkC, PF1784

Species: Pyrococcus furiosus

Subunit composition of ADP-dependent phosphofructokinase = [PfkA]4
         ADP-dependent phosphofructokinase subunit = PfkA

Summary:
ADP-dependent phosphofructokinase and ADP-dependent glucokinase are members of a unique family unrelated to bacterial ATP-dependent glucokinase, or eukaryotic hexokinase (reviewed in [Verhees03]).

The native molecular mass of the enzyme partially purified from cell-free extracts of Pyrocuccus furiosus was determined by gel filtration chromatography [Tuininga99].
The subunit molecular mass of the purified, recombinant protein was determined by SDS-PAGE [Tuininga99].

Gene Citations: [Kengen01]

Molecular Weight of Polypeptide: 52.337 kD (from nucleotide sequence), 52 kD (experimental) [Tuininga99 ]

Molecular Weight of Multimer: 180 kD (experimental) [Tuininga99]

Unification Links: ModBase:Q9V2Z7 , Pride:Q9V2Z7 , Protein Model Portal:Q9V2Z7 , SMR:Q9V2Z7 , String:186497.PF1784 , Swiss-Model:Q9V2Z7 , UniProt:Q9V2Z7

Relationship Links: Entrez-Nucleotide:PART-OF:AF127909 , InterPro:IN-FAMILY:IPR007666 , InterPro:IN-FAMILY:IPR011790 , InterPro:IN-FAMILY:IPR015990 , Panther:IN-FAMILY:PTHR21208 , Pfam:IN-FAMILY:PF04587 , Prosite:IN-FAMILY:PS51255

Gene-Reaction Schematic: ?


Enzymatic reaction of: ADP-dependent phosphofructokinase

EC Number: 2.7.1.146

β-D-fructofuranose 6-phosphate + ADP <=> fructose 1,6-bisphosphate + AMP + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

This reaction is reversible.

Alternative Substrates for ADP: GDP [Tuininga99 ]

In Pathways: glycolysis V (Pyrococcus)

Summary:
Enzyme activity data were derived from purified, recombinant protein expressed in Escherichia coli. The Km values were determined at 50 deg. C [Tuininga99].

Cofactors or Prosthetic Groups: Co2+ [Tuininga99], Mn2+ [Tuininga99], Mg2+ [Tuininga99]

Inhibitors (Competitive): AMP [Tuininga99] , ATP [Tuininga99]

Inhibitors (Unknown Mechanism): sodium chloride [Tuininga99] , potassium chloride [Tuininga99]

Kinetic Parameters:

Substrate
Km (μM)
Citations
β-D-fructofuranose 6-phosphate
2300.0
[Tuininga99]
ADP
110.0
[Tuininga99]

pH(opt): 6.5 [Tuininga99]


References

Kengen01: Kengen SW, Tuininga JE, Verhees CH, van der Oost J, Stams AJ, de Vos WM (2001). "ADP-dependent glucokinase and phosphofructokinase from Pyrococcus furiosus." Methods Enzymol 331;41-53. PMID: 11265478

Tuininga99: Tuininga JE, Verhees CH, van der Oost J, Kengen SW, Stams AJ, de Vos WM (1999). "Molecular and biochemical characterization of the ADP-dependent phosphofructokinase from the hyperthermophilic archaeon Pyrococcus furiosus." J Biol Chem 274(30);21023-8. PMID: 10409652

Verhees03: Verhees CH, Kengen SW, Tuininga JE, Schut GJ, Adams MW, De Vos WM, Van Der Oost J (2003). "The unique features of glycolytic pathways in Archaea." Biochem J 375(Pt 2);231-46. PMID: 12921536


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Fri Dec 26, 2014, biocyc11.