Any feedback?
Literature summary for 4.2.1.11 extracted from
- Effects of the G376E and G157D mutations on the stability of yeast enolase - a model for human muscle enolase deficiency (2007), FEBS J., 275, 97-106.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| inserted into pET-3a, expressed in Escherichia coli BL21-DE3, site-directed mutagenesis performed | Saccharomyces cerevisiae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| G157D | correctly folded, less stable than wild-type enolase, dissociation into subunit forms accelerated | Saccharomyces cerevisiae |
| G376E | correctly folded, less stable than wild-type enolase, dissociation into subunit forms accelerated | Saccharomyces cerevisiae |
| additional information | folding studies, dissociation experiments, determination of thermal and enzymatic stability | Saccharomyces cerevisiae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-phospho-D-glycerate | Saccharomyces cerevisiae | - |
phosphoenolpyruvate + H2O | - |
r |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | P00924 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant proteins, SDS-PAGE | Saccharomyces cerevisiae |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
enzyme activity monitored by following the conversion of phosphoenolpyruvate to 2-phospho-D-glycerate, specific activities of the variants, relative to wildtype enolase, are 0.1% for G157D and 0.01% for G376E | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-phospho-D-glycerate | - |
Saccharomyces cerevisiae | phosphoenolpyruvate + H2O | - |
r | |
| 2-phospho-D-glycerate | influence on exchange of amino acid residues on structure, dissociation and function of enolase analyzed | Saccharomyces cerevisiae | phosphoenolpyruvate + H2O | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | subunit dissociation of wild-type and G157D enolases by incubation with NaClO4 at 15°C for 24 h, spectrometrically measured | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| enolase | - |
Saccharomyces cerevisiae |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
thermal stability lower in mutant forms of enolase, wild-type enolase has Tm of 55.4°C, whereas G367E and G157D reveals a Tm of 51.2°C and 49.9°C, respectively, addition of 50 microM phosphonoacetohydroxamate increases thermal stabilization of wildtype and G157D enolases, but not of G367E | Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.1 | - |
activity assay at | Saccharomyces cerevisiae |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
