PFK2/YMR205C Summary Help

Standard Name PFK2 1
Systematic Name YMR205C
Feature Type ORF, Verified
Description Beta subunit of heterooctameric phosphofructokinase; involved in glycolysis; indispensable for anaerobic growth; activated by fructose-2,6-bisphosphate and AMP; mutation inhibits glucose induction of cell cycle-related genes (2, 3, 4, 5, 6, 7, 8 and see Summary Paragraph)
Name Description PhosphoFructoKinase 9
Chromosomal Location
ChrXIII:674766 to 671887 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Genetic position: 132 cM
Gene Ontology Annotations All PFK2 GO evidence and references
  View Computational GO annotations for PFK2
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 12 genes
Classical genetics
reduction of function
Large-scale survey
189 total interaction(s) for 169 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 41
  • Affinity Capture-RNA: 3
  • Affinity Capture-Western: 1
  • Biochemical Activity: 7
  • PCA: 2
  • Protein-peptide: 3
  • Reconstituted Complex: 4
  • Two-hybrid: 2

Genetic Interactions
  • Negative Genetic: 102
  • Phenotypic Enhancement: 1
  • Phenotypic Suppression: 1
  • Positive Genetic: 9
  • Synthetic Growth Defect: 7
  • Synthetic Lethality: 4
  • Synthetic Rescue: 2

Expression Summary
Length (a.a.) 959
Molecular Weight (Da) 104,617
Isoelectric Point (pI) 6.65
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXIII:674766 to 671887 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Genetic position: 132 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..2880 674766..671887 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000004818

PFK1 and PFK2 encode the alpha and beta subunits, respectively, of phosphofructokinase (Pfk-1), a key enzyme of glycolysis that catalyzes the formation of fructose 1,6-bisphosphate from fructose 6-phosphate and ATP (10, 11). Unlike other enzymes of glycolysis, phosphofructokinase and pyruvate kinase (Cdc19p, Pyk2p) only function in the forward direction; hence these enzymes are specific to glycolysis and are not involved in gluconeogenesis.

Glycolysis is the lysis, or splitting, of one molecule of glucose into two molecules of pyruvate, producing a net gain of two ATP molecules. Pyruvate can then be used in anaerobic (fermentation) or aerobic (respiration) metabolism. The glycolysis pathway and the genes involved are illustrated here.

Phosphofructokinase is a hetero-oligomeric enzyme composed of four alpha and four beta subunits, arranged as four heterodimers of alpha-beta (12, 13, 6). Electron microscopy studies at 2 nm resolution revealed that the three-dimensional structure consists of two quasi-equivalent tetramers in which four alpha subunits form the central core of the octamer (14). The amino acid sequences of Pfk1p and Pfk2p exhibit 20% homology between the N- and the C-terminal halves for each subunit and 55% homology between the two subunits overall. Although biochemical analysis indicated that the beta subunits contain binding sites for the substrate fructose 6-phosphate and hence confer the catalytic activity of the enzyme (15), more recent mutant studies have shown that each subunit (alpha and beta) has both a catalytic and a regulatory function (2).

Studies on the regulation of glycolytic genes indicate that glucose strongly induces PFK2 and PFK1 mRNA synthesis (16). This induction facilitates production of phosphofructokinase during a shift from gluconeogenesis to glycolysis. Phosphofructokinase activity is also subject to allosteric control, with ATP inhibiting the enzyme and AMP, as well as fructose 2,6-bisphosphate, reversing the inhibition (17, 18). Allosteric control is abolished by a single point mutation in either subunit, which impairs growth on gluconeogenic carbon sources but does not affect growth on glucose. This suggests that the main function of the allosteric regulation is to facilitate growth in changing environments (19).

PFK1 and PFK2 show significant homology to PFK subunits from mammals and bacteria (9). Analysis of these PFK sequences has led to the hypothesis that two gene duplication events occurred in the evolution of the yeast PFK genes: the first event occurred soon after the separation of prokaryotic and eukaryotic lineage, and the second took place in Saccharomyces later (9). Although Pfk protein sequences are conserved, the oligomeric structure of the functional enzyme varies among organisms, with homotetramers found in bacteria and mammals, homooctamers in S. pombe, and heterooctamers in S. cerevsiae and K. lactis (reviewed in 20) . In humans, mutation in the muscle isoenzyme of Pfk causes glycogen storage disease VII, also called Tarui disease (OMIM; 21 and references therein).

Note: PFK1 and PFK2 nomenclature is reversed in some earlier studies (see PMID:1387501, for example) relative to that used now.

Last updated: 2006-07-31 Contact SGD

References cited on this page View Complete Literature Guide for PFK2
1) Parmar L, et al.  (1984) Multiple genes control particulate phosphofructokinase of yeast. Mol Gen Genet 197(3):515-6
2) Arvanitidis A and Heinisch JJ  (1994) Studies on the function of yeast phosphofructokinase subunits by in vitro mutagenesis. J Biol Chem 269(12):8911-8
3) Lobo Z and Maitra PK  (1983) Phosphofructokinase mutants of yeast. Biochemistry and genetics. J Biol Chem 258(3):1444-9
4) Kriegel T, et al.  (1987) Hydrodynamic studies on the quaternary structure of reacting yeast phosphofructokinase. Biomed Biochim Acta 46(5):349-55
5) Otto A, et al.  (1986) Kinetic effects of fructose-1,6-bisphosphate on yeast phosphofructokinase. Biomed Biochim Acta 45(7):865-75
6) Nissler K, et al.  (1985) An electron microscopy study of the quarternary structure of yeast phosphofructokinase. Biomed Biochim Acta 44(2):251-9
7) Newcomb LL, et al.  (2003) Glucose regulation of Saccharomyces cerevisiae cell cycle genes. Eukaryot Cell 2(1):143-9
8) Foy JJ and Bhattacharjee JK  (1978) Biosynthesis and regulation of fructose-1,6-bisphosphatase and phosphofructokinase in Saccharomyces cerevisiae grown in the presence of glucose and gluconeogenic carbon sources. J Bacteriol 136(2):647-56
9) Heinisch J, et al.  (1989) The phosphofructokinase genes of yeast evolved from two duplication events. Gene 78(2):309-21
10) Heinisch J  (1986) Isolation and characterization of the two structural genes coding for phosphofructokinase in yeast. Mol Gen Genet 202(1):75-82
11) Clifton D and Fraenkel DG  (1982) Mutant studies of yeast phosphofructokinase. Biochemistry 21(8):1935-42
12) Kopperschlager G, et al.  (1976) Studies on the oligomeric structure of yeast phosphofructo-kinase by means of cross-linking diimidoesters. Biochem Biophys Res Commun 71(1):371-8
13) Kopperschlager G, et al.  (1977) Physicochemical parameters and subunit composition of yeast phosphofructokinase. Eur J Biochem 81(2):317-25
14) Burgers PM, et al.  (1988) Exonuclease V from Saccharomyces cerevisiae. A 5'----3'-deoxyribonuclease that produces dinucleotides in a sequential fashion. J Biol Chem 263(17):8099-105
15) Tijane MN, et al.  (1980) Sulfhydryl groups of yeast phosphofructokinase-specific localization on beta subunits of fructose 6-phosphate binding sites as demonstrated by a differential chemical labeling study. J Biol Chem 255(21):10188-93
16) Moore PA, et al.  (1991) Yeast glycolytic mRNAs are differentially regulated. Mol Cell Biol 11(10):5330-7
17) Simonis N, et al.  (2004) Combining pattern discovery and discriminant analysis to predict gene co-regulation. Bioinformatics 20(15):2370-9
18) Farooqui J, et al.  (1980) In vivo studies on yeast cytochrome c methylation in relation to protein synthesis. J Biol Chem 255(10):4468-73
19) Rodicio R, et al.  (2000) Single point mutations in either gene encoding the subunits of the heterooctameric yeast phosphofructokinase abolish allosteric inhibition by ATP. J Biol Chem 275(52):40952-60
20) Schwock J, et al.  (2004) Interaction of 6-phosphofructokinase with cytosolic proteins of Saccharomyces cerevisiae. Yeast 21(6):483-94
21) Raben N, et al.  (1995) Functional expression of human mutant phosphofructokinase in yeast: genetic defects in French Canadian and Swiss patients with phosphofructokinase deficiency. Am J Hum Genet 56(1):131-41