Recombinant Neurospora crassa Triosephosphate isomerase (tpi-1)
Description
Definition and Basic Properties
Recombinant tpi-1 is a recombinant protein produced through heterologous expression systems, typically in E. coli or yeast. It retains the catalytic function and structural integrity of the native enzyme, with modifications to enhance stability or solubility for research applications. Key properties include:
| Property | Value/Description |
|---|---|
| Uniprot ID | Q7S2Z9 |
| Molecular Weight | ~26–27 kDa (SDS-PAGE) |
| Purity | >85% (SDS-PAGE) |
| Storage Conditions | -20°C/-80°C (lyophilized form stable for 12 months) |
| Source Organism | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A) |
Data sourced from product specifications and genome annotations .
Functional Role
Triosephosphate isomerases are central to glycolysis and gluconeogenesis. In Neurospora, tpi-1 likely participates in:
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Glycolytic Pathway: Facilitating rapid energy production under aerobic/anaerobic conditions.
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Metabolic Regulation: Interacting with upstream/downstream enzymes (e.g., aldolase, glyceraldehyde-3-phosphate dehydrogenase).
Catalytic Mechanism
While direct kinetic data for tpi-1 is limited, TIMs generally follow a proton transfer mechanism:
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Substrate Binding: DHAP binds to the active site via hydrogen bonds.
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Catalytic Step: Lysine (K10) abstracts a proton from C2 of DHAP, forming an enolate intermediate.
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Product Release: The enolate tautomerizes to G3P, releasing the product .
Recombinant Expression Systems
tpi-1 is often expressed in heterologous hosts for biochemical studies. Key findings include:
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E. coli Expression: Yields functional protein but may lack post-translational modifications (e.g., phosphorylation) critical for activity .
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Yeast Systems: Disruption of glycosylation pathways (OCH1, MNN9) enhances secretion efficiency, potentially applicable to tpi-1 production .
Challenges and Future Directions
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Structural Elucidation: No crystal structure of tpi-1 has been reported; homology modeling is required for precise functional insights.
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Post-Translational Modifications: Phosphorylation or glycosylation may regulate tpi-1 activity, necessitating studies in native N. crassa systems .
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Industrial Applications: Engineering tpi-1 for thermostability or substrate specificity could expand its utility in bioindustrial processes.
Product Specs
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