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Literature summary for 3.8.1.3 extracted from
- MDP-1 is a new and distinct member of the haloacid dehalogenase family of aspartate-dependent phosphohydrolases (2001), Biochemistry, 40, 12704-12711.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli BL21(DE3) of wild-type and mutant enzymes fused to the calmodulin binding peptide CBP from mouse or to CBP and FLAG from yeast | Saccharomyces cerevisiae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D10E | site-directed mutagenesis, inactive catalytic site residue mutant | Saccharomyces cerevisiae |
| D10N | site-directed mutagenesis, inactive catalytic site residue mutant | Saccharomyces cerevisiae |
| D121N | site-directed mutagenesis, catalytic site residue mutant, 0.4% activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
| D122N | site-directed mutagenesis, catalytic site residue mutant, 0.1% activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
| D12N | site-directed mutagenesis, catalytic site residue mutant, 8% activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
| K99R | site-directed mutagenesis, catalytic site residue mutant, 1.4% activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
| N126D | site-directed mutagenesis, 52% activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
| S68A | site-directed mutagenesis, catalytic site residue mutant, 0.1% activity compared to the wild-type enzyme | Saccharomyces cerevisiae |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | dependent on | Saccharomyces cerevisiae |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type and mutant fusion proteins from Escherichia coli, the tags are removed | Saccharomyces cerevisiae |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| haloacetate + H2O = glycolate + halide | enzyme contains the conserved motif Asp-Xaa-Asp-Xaa-Thr, open reaction conformation | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the domain proximal to the active site which is responsible for important specific interaction of low molecular weight substrates with the enzymes of the haloacid dehalogenase superfamily is missing in MDP-1, thus the enzyme is able to utilize also large substrates such as proteins | Saccharomyces cerevisiae | ? | - |
? | |
| tyrosine-phosphorylated proteins + H2O | - |
Saccharomyces cerevisiae | protein + phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the domain proximal to the active site which is responsible for important specific interaction of low molecular weight substrates with the enzymes of the haloacid dehalogenase superfamily is missing in MDP-1, comparison of domain structures within the enzyme family | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| magnesium-dependent acid phosphatase-1 | - |
Saccharomyces cerevisiae |
| MDP-1 | - |
Saccharomyces cerevisiae |
| More | the enzyme belongs to the haloacid dehalogenase HAD superfamily of enzymes | Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | - |
assay at | Saccharomyces cerevisiae |
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Release 2023.1 (January 2023)
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