TPI1

TPI1

Target · Glycolytic enzyme

TPI1 Triosephosphate isomerase 1 · Triosephosphate isomerase

TPI1 (triosephosphate isomerase 1) is a cytoplasmic glycolytic enzyme that interconverts glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. It is a homodimer, and mutations in the TPI1 gene are associated with triosephosphate isomerase deficiency. Browse Assay Genie's current range of TPI1 research reagents below, or read on for the biology behind the target.

Cytoplasmic enzymeGlycolysis and gluconeogenesisLinked to TPI deficiency
249 aa
Protein length
~27 kDa
Molecular weight
12p13.31
Gene locus
EC 5.3.1.1
Enzyme class
Target information

What is TPI1 (triosephosphate isomerase 1)?

TPI1 is an enzyme that catalyses the isomerisation of glyceraldehyde 3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP). This reaction operates in both glycolysis and gluconeogenesis, linking the two three-carbon intermediates so that both can be channelled through the pathway. The active enzyme consists of two identical protein subunits, and the TPI1 protein belongs to the triosephosphate isomerase family.

UniProt also notes that the enzyme is responsible for the non-negligible production of methylglyoxal. This is a reactive, cytotoxic side-product that can modify and alter proteins, DNA and lipids, so TPI1 is of interest not only for central carbon metabolism but also for the study of metabolic by-products and cellular damage. In the cell, the protein is found in the cytoplasm.

The human TPI1 gene lies on chromosome 12 and is recorded by HGNC as triosephosphate isomerase 1. According to the NCBI Gene summary, mutations in this gene are associated with triosephosphate isomerase deficiency. Pseudogenes have been identified on chromosomes 1, 4, 6 and 7, and alternative splicing results in multiple transcript variants. Orthologues are annotated in mouse and rat, both named Tpi1, which allows comparative work in rodent models.

Glycolysis and metabolism

TPI1 catalyses the interconversion of G3P and DHAP, making it a core enzyme for studying glycolytic and gluconeogenic flux.

Inherited metabolic disease

Mutations in the TPI1 gene are associated with triosephosphate isomerase deficiency, making the enzyme relevant to disease-focused research.

Methylglyoxal and cell damage

TPI1 contributes to methylglyoxal production, a reactive side-product that can modify proteins, DNA and lipids.

Gene and transcript analysis

Multiple transcript variants and pseudogenes on several chromosomes make TPI1 a useful subject for gene expression and splicing studies.

Background

TPI1 frequently asked questions

What does TPI1 do?

TPI1 catalyses the isomerisation of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate in glycolysis and gluconeogenesis. It functions as a homodimer in the cytoplasm. UniProt also notes that it contributes to production of methylglyoxal, a reactive cytotoxic side-product.

What is TPI1 also called, and does it have isoforms?

HGNC names the gene triosephosphate isomerase 1, and UniProt names the protein triosephosphate isomerase. No alternative symbols are listed. The NCBI Gene summary states that alternative splicing results in multiple transcript variants, and that pseudogenes exist on chromosomes 1, 4, 6 and 7.

Is TPI1 linked to disease and conserved in rodents?

Mutations in the TPI1 gene are associated with triosephosphate isomerase deficiency. Orthologues named Tpi1 are annotated in both mouse and rat. Check the datasheet of any product for its validated reactivity.

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Related targets

Other glycolytic enzymes and metabolic pathway targets with products at Assay Genie.

Gene and protein annotations from HGNC, NCBI Gene and UniProt P60174; product specifications from Assay Genie datasheets.

TPI1 Product listing