PGK1 BASIC INFORMATION
| Standard Name | PGK1 |
|---|---|
| Systematic Name | YCR012W |
| Feature Type | ORF, Verified |
| Description | 3-phosphoglycerate kinase, catalyzes transfer of high-energy phosphoryl groups from the acyl phosphate of 1,3-bisphosphoglycerate to ADP to produce ATP; key enzyme in glycolysis and gluconeogenesis (1, 2 and see Summary Paragraph)
|
| Name Description | 3-PhosphoGlycerate Kinase |
| GO Annotations | All PGK1 GO evidence and references |
|---|---|
| View Computational GO annotations for PGK1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated | |
| High-throughput |
| Pathways |
|---|
| Mutant Phenotype | All PGK1 Phenotype details and references |
|---|---|
| Classical genetics | |
| null | |
| overexpression | |
| Large-scale survey | |
| null |
| Interactions | PGK1 All interactions details and references |
|---|---|
| 47 total interaction(s) for 44 unique genes/features. | |
| Physical Interactions |
|
| Genetic Interactions |
|
| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB |
|---|
| Primary SGDID | S000000605 |
|---|
ADDITIONAL INFORMATION for PGK1
SUMMARY PARAGRAPH for PGK1
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.
During glycolysis, Pgk1p (3-phosphoglycerate kinase) catalyzes the transfer of a high-energy phosphoryl group from the acyl phosphate of 1,3-diphosphoglycerate to ADP to produce ATP. Pgk1p also catalyzes the reverse reaction during gluconeogenesis wherein 3-phosphoglycerate and ATP are converted to 1,3-diphosphoglycerate and ADP (2, 3). The reversible reaction is catalyzed in the presence of magnesium ions.
Gluconeogenesis is the process whereby glucose is synthesized from non-carbohydrate precursors, which enables yeast cells to grow on non-sugar carbon sources like ethanol, glycerol, or peptone. The reactions of gluconeogenesis, shown here, mediate conversion of pyruvate to glucose, which is the opposite of glycolysis, the formation of pyruvate from glucose. While these two pathways have several reactions in common, they are not the exact reverse of each other. As the glycolytic enzymes phosphofructokinase (Pfk1p, Pfk2p) and pyruvate kinase (Cdc19p) only function in the forward direction, the gluconeogenesis pathway replaces those steps with the enzymes pyruvate carboxylase (Pyc1p, Pyc2p) and phosphoenolpyruvate carboxykinase (Pck1p)-generating oxaloacetate as an intermediate from pyruvate to phosphoenolpyruvate-and also the enzyme fructose-1,6-bisphosphatase (Fbp1p) (reviewed in 4). Overall, the gluconeogenic reactions convert two molecules of pyruvate to a molecule of glucose, with the expenditure of six high-energy phosphate bonds, four from ATP and two from GTP.
Pgk1p is composed of two structurally similar domains linked by a helical hinge that also interact through a C-terminal helix (5). Purification of Pgk1p from a variety of organisms indicates that it has been highly conserved throughout evolution (6).
PGK1 is abundantly expressed in cells growing in glucose, and transcription is increased by heat shock (7). In contrast, mRNA levels are low in cells grown in pyruvate, acetate, or lactate, although the message stability is not affected by the carbon source (8, 9). Transcription is activated by the transcription factors Rap1p, Abf1p, and Reb1p, which each bind to sequences in the PGK1 promoter (8, 10). Because PGK1 is a highly-expressed gene and its mRNA is relatively stable, it has been the subject of a large number of studies on mRNA stability and decay, codon bias, and protein structure, folding, and kinetics (see Literature Guide for a complete listing).
REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for PGK1]
| 1) | Blake CC and Rice DW (1981) Phosphoglycerate kinase. Philos Trans R Soc Lond B Biol Sci 293(1063):93-104 |
| 2) | Hitzeman RA, et al. (1980) Isolation and characterization of the yeast 3-phosphoglycerokinase gene (PGK) by an immunological screening technique. J Biol Chem 255(24):12073-80 |
| 3) | Lam KB and Marmur J (1977) Isolation and characterization of Saccharomyces cerevisiae glycolytic pathway mutants. J Bacteriol 130(2):746-9 |
| 4) | Klein CJ, et al. (1998) Glucose control in Saccharomyces cerevisiae: the role of Mig1 in metabolic functions. Microbiology 144 ( Pt 1):13-24 |
| 5) | Watson HC, et al. (1982) Sequence and structure of yeast phosphoglycerate kinase. EMBO J 1(12):1635-40 |
| 6) | Fifis T and Scopes RK (1978) Purification of 3-phosphoglycerate kinase from diverse sources by affinity elution chromatography. Biochem J 175(1):311-9 |
| 7) | Piper PW, et al. (1986) Transcription of the phosphoglycerate kinase gene of Saccharomyces cerevisiae increases when fermentative cultures are stressed by heat-shock. Eur J Biochem 161(3):525-31 |
| 8) | Chambers A, et al. (1989) Transcriptional control of the Saccharomyces cerevisiae PGK gene by RAP1. Mol Cell Biol 9(12):5516-24 |
| 9) | Moore PA, et al. (1991) Yeast glycolytic mRNAs are differentially regulated. Mol Cell Biol 11(10):5330-7 |
| 10) | Packham EA, et al. (1996) The multifunctional transcription factors Abf1p, Rap1p and Reb1p are required for full transcriptional activation of the chromosomal PGK gene in Saccharomyces cerevisiae. Mol Gen Genet 250(3):348-56 |




