Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

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 Sat Nov 22, 2014, BIOCYC13B.