PFK27/YOL136C Summary Help

Standard Name PFK27 1
Systematic Name YOL136C
Feature Type ORF, Verified
Description 6-phosphofructo-2-kinase; catalyzes synthesis of fructose-2,6-bisphosphate; inhibited by phosphoenolpyruvate and sn-glycerol 3-phosphate, expression induced by glucose and sucrose, transcriptional regulation involves protein kinase A (1, 2, 3, 4 and see Summary Paragraph)
Also known as: PFK-2
Name Description 6-PhosphoFructo-2-Kinase 1
Chromosomal Location
ChrXV:68754 to 67561 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All PFK27 GO evidence and references
  View Computational GO annotations for PFK27
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 5 genes
Large-scale survey
39 total interaction(s) for 31 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 6
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 1
  • Biochemical Activity: 2
  • Reconstituted Complex: 1
  • Two-hybrid: 2

Genetic Interactions
  • Dosage Growth Defect: 9
  • Dosage Lethality: 1
  • Negative Genetic: 11
  • Positive Genetic: 4

Expression Summary
Length (a.a.) 397
Molecular Weight (Da) 45,317
Isoelectric Point (pI) 5.47
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXV:68754 to 67561 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2006-01-05 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1194 68754..67561 2006-01-05 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 SGDIDS000005496

PFK27 and PFK26 encode two isozymes of 6-phosphofructo-2-kinase, which catalyzes synthesis of fructose-2,6-bisphosphate (F2,6bP) from fructose-6-phosphate and ATP (1, 5). F2,6bP is a strong positive allosteric effector of the glycolytic enzyme phosphofructokinase (Pfk1p and Pfk2p; 6, 7), and thus is important for regulation of glycolysis. F2,6bP is also an inhibitor of the gluconeogenic enzyme fructose-1,6-bisphosphatase (Fbp1p), although the physiological significance of this inhibition is not yet clear (8).

PFK27 synthesis is induced by fermentable carbon sources, while Pfk26p is activated by protein kinase A phosphorylation (5). Deletion of either PFK26 or PFK27 does not confer a detectable growth phenotype (1, 9). Moreover, although pfk26 pfk27 double mutant cells do not synthesize F2,6bP, they grow normally on fermentable sugars and exhibit normal flux rates for glucose utilization and production of ethanol (1). Metabolic studies of glycolytic intermediates in exponential phase cells reveal elevated levels of fructose-6-phosphate and decreased ATP/ADP ratios in pfk26 and pfk27 single mutants relative to wild type (9).

In mammals, 6-phosphofructo-2-kinase is synthesized with fructose-2,6-bisphosphatase as single bifunctional polypeptide. Isozymes of this protein are found in different tissues and are encoded by four genes: PFKFB1, PFKFB2, PFKFB3, and PFKFB4 (reviewed in 10). This bifunctional enzyme structure has been found in many other eukaryotes, including Arabidopsis and Drosophila, and in the prokaryote Desulfovibrio desulfuricans. The S. cerevisiae PFK26 gene also would appear to encode a bifunctional enzyme, however the fructose-2,6-bisphosphatase moiety is inactive (3).

Last updated: 2006-07-07 Contact SGD

References cited on this page View Complete Literature Guide for PFK27
1) Boles E, et al.  (1996) Cloning of a second gene encoding 5-phosphofructo-2-kinase in yeast, and characterization of mutant strains without fructose-2,6-bisphosphate. Mol Microbiol 20(1):65-76
2) Goncalves PM, et al.  (1997) Signalling pathways leading to transcriptional regulation of genes involved in the activation of glycolysis in yeast. Mol Microbiol 25(3):483-93
3) Kretschmer M, et al.  (1993) Mutation of monofunctional 6-phosphofructo-2-kinase in yeast to bifunctional 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase. Biochemistry 32(41):11143-8
4) Bedri A, et al.  (1989) Kinetics of 6-phosphofructo-2-kinase from Saccharomyces cerevisiae: inhibition of the enzyme by ATP. Biomed Biochim Acta 48(7):403-11
5) Kretschmer M and Fraenkel DG  (1991) Yeast 6-phosphofructo-2-kinase: sequence and mutant. Biochemistry 30(44):10663-72
6) Otto A, et al.  (1986) Kinetic effects of fructose-1,6-bisphosphate on yeast phosphofructokinase. Biomed Biochim Acta 45(7):865-75
7) Heinisch JJ, et al.  (1996) A yeast phosphofructokinase insensitive to the allosteric activator fructose 2,6-bisphosphate. Glycolysis/metabolic regulation/allosteric control. J Biol Chem 271(27):15928-33
8) Muller S, et al.  (1997) Mutant studies of phosphofructo-2-kinases do not reveal an essential role of fructose-2,6-bisphosphate in the regulation of carbon fluxes in yeast cells. Microbiology 143 ( Pt 9):3055-61
9) Raamsdonk LM, et al.  (2001) A functional genomics strategy that uses metabolome data to reveal the phenotype of silent mutations. Nat Biotechnol 19(1):45-50
10) Rider MH, et al.  (2004) 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: head-to-head with a bifunctional enzyme that controls glycolysis. Biochem J 381(Pt 3):561-79