TPI1/YDR050C Summary Help

TPI1 BASIC INFORMATION

Standard Name TPI1
Systematic Name YDR050C
Feature Type ORF, Verified
Description Triose phosphate isomerase, abundant glycolytic enzyme; mRNA half-life is regulated by iron availability; transcription is controlled by activators Reb1p, Gcr1p, and Rap1p through binding sites in the 5' non-coding region (1, 2, 3 and see Summary Paragraph)
Name Description Triose-Phosphate Isomerase 3
GO Annotations All TPI1 GO evidence and references
    View Computational GO annotations for TPI1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Pathways
Mutant Phenotype All TPI1 Phenotype details and references
Classical genetics
conditional
Large-scale survey
null
Interactions TPI1 All interactions details and references
21 total interaction(s) for 18 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 13
  • Affinity Capture-RNA: 1
  • Co-crystal Structure: 1
  • Reconstituted Complex: 2
Genetic Interactions
  • Synthetic Growth Defect: 3
  • Synthetic Lethality: 1
Sequence Information
ChrIV:556471 to 555725 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Last Update Coordinates: 2008-06-05 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..747 556471..555725 2008-06-05 1996-07-31
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000002457

TPI1 RESOURCES

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SGD ORF map
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Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for TPI1

SUMMARY PARAGRAPH for TPI1

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, Tpi1p (triose phosphate isomerase) catalyzes the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate (3, 4). It is required for growth on glucose as the sole carbon source (4). In Saccharomyces cerevisiae, Tpi1p is an abundant glycolytic enzyme that makes up about 2% of the soluble cellular protein (2).

Tpi1p functions as a homodimer (5) and the active site residues include Glu165, His95, and Lys12. The catalytic site Glu and His residues are thought to extract and donate protons during catalysis (5, 6). The sequence around the active site residues is fully conserved in a number of organisms including chicken, yeast and Trypanosoma brucei (7).

The expression of TPI1 may be regulated by the transcriptional activators Reb1p, Rap1p, and Gcr1p that bind sites in the 5' non-coding region of TPI1. However, Gcr1p is able to activate gene expression in the absence of Reb1p or Rap1p. Therefore, it has been suggested that Gcr1p is required for activation of TPI1 and that the role of Reb1p and Rap1p, which bind adjacent to Gcr1p-binding sites, may be to facilitate or modulate Gcr1p binding in vivo (2).

In humans, deficiency of triosephosphate isomerase (TPI1) (OMIM) causes haemolytic anaemia coupled with progressive, severe neurological disorder (8).

Last updated: 2006-07-31

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for TPI1]

1) Krieger K and Ernst JF  (1994) Iron regulation of triosephosphate isomerase transcript stability in the yeast Saccharomyces cerevisiae. Microbiology 140 ( Pt 5):1079-84
2) Scott EW and Baker HV  (1993) Concerted action of the transcriptional activators REB1, RAP1, and GCR1 in the high-level expression of the glycolytic gene TPI. Mol Cell Biol 13(1):543-50
3) Alber T and Kawasaki G  (1982) Nucleotide sequence of the triose phosphate isomerase gene of Saccharomyces cerevisiae. J Mol Appl Genet 1(5):419-34
4) Compagno C, et al.  (2001) Alterations of the glucose metabolism in a triose phosphate isomerase-negative Saccharomyces cerevisiae mutant. Yeast 18(7):663-70
5) Lolis E, et al.  (1990) Structure of yeast triosephosphate isomerase at 1.9-A resolution. Biochemistry 29(28):6609-18
6) Joseph-McCarthy D, et al.  (1994) Crystal structure of the mutant yeast triosephosphate isomerase in which the catalytic base glutamic acid 165 is changed to aspartic acid. Biochemistry 33(10):2824-9
7) Wierenga RK, et al.  (1992) Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase. J Mol Biol 224(4):1115-26
8) Olah J, et al.  (2002) Triosephosphate isomerase deficiency: a neurodegenerative misfolding disease. Biochem Soc Trans 30(2):30-8