Literature summary extracted from
Zhao, S.; Choy, B.S.; Kornblatt, M.J.
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)
EC Number |
Cloned (Comment) |
Organism |
---|
4.2.1.11 |
inserted into pET-3a, expressed in Escherichia coli BL21-DE3, site-directed mutagenesis performed |
Saccharomyces cerevisiae |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
4.2.1.11 |
G157D |
correctly folded, less stable than wild-type enolase, dissociation into subunit forms accelerated |
Saccharomyces cerevisiae |
4.2.1.11 |
G376E |
correctly folded, less stable than wild-type enolase, dissociation into subunit forms accelerated |
Saccharomyces cerevisiae |
4.2.1.11 |
additional information |
folding studies, dissociation experiments, determination of thermal and enzymatic stability |
Saccharomyces cerevisiae |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
4.2.1.11 |
2-phospho-D-glycerate |
Saccharomyces cerevisiae |
- |
phosphoenolpyruvate + H2O |
- |
r |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.2.1.11 |
Saccharomyces cerevisiae |
P00924 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
4.2.1.11 |
recombinant proteins, SDS-PAGE |
Saccharomyces cerevisiae |
Source Tissue
EC Number |
Source Tissue |
Comment |
Organism |
Textmining |
---|
Specific Activity [micromol/min/mg]
EC Number |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Comment |
Organism |
---|
4.2.1.11 |
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)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
4.2.1.11 |
2-phospho-D-glycerate |
- |
Saccharomyces cerevisiae |
phosphoenolpyruvate + H2O |
- |
r |
|
4.2.1.11 |
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
EC Number |
Subunits |
Comment |
Organism |
---|
4.2.1.11 |
More |
subunit dissociation of wild-type and G157D enolases by incubation with NaClO4 at 15°C for 24 h, spectrometrically measured |
Saccharomyces cerevisiae |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
4.2.1.11 |
enolase |
- |
Saccharomyces cerevisiae |
Temperature Stability [°C]
EC Number |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
---|
4.2.1.11 |
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
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
4.2.1.11 |
7.1 |
- |
activity assay at |
Saccharomyces cerevisiae |