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Literature summary for 4.2.1.22 extracted from
- Functional rescue of mutant human cystathionine ß-synthase by manipulation of Hsp26 and Hsp70 levels in Saccharomyces cerevisiae (2009), J. Biol. Chem., 284, 4238-4245.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| a mutant form of the human cystathionine beta-synthase protein, I278T, is expressed in Saccharomyces cerevisiae | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| I278T | I278T mutant is expressed in Saccharomyces cerevisiae. By manipulation of the cellular chaperone environment the enzymatic function is resuced. Ethanol treatment induces Hsp70 and causes increased activity and steady-state levels of I278T. Exposure of I278T yeast to a 45°C heat shock for 3 h results in a 312% increase in steady-state CBS and a 511% increase in CBS activity. Hsp70 and Hsp26 bind specifically to I278T. Deletion of the SSA2 gene, which encodes a cytoplasmic isoform of Hsp70, eliminates the ability of ethanol to restore function, indicating that Hsp70 plays a positive role in proper I278T folding. In contrast, deletion of HSP26 results in increased I278T protein and activity, whereas overexpression of Hsp26 results in reduced I278T protein. The Hsp26-I278T complex is degraded via a ubiquitin/proteosome-dependent mechanism | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CBS | - |
Homo sapiens |
| cystathionine beta-synthase | - |
Homo sapiens |
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