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Literature summary for 3.1.1.75 extracted from
- To be or not to be a poly(3-hydroxybutyrate) (PHB) depolymerase: PhaZd1 (PhaZ6) and PhaZd2 (PhaZ7) of Ralstonia eutropha, highly active PHB depolymerases with no detectable role in mobilization of accumulated PHB (2014), Appl. Environ. Microbiol., 80, 4936-4946.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | activates alone, but inhibits in presence of divalent cations | Cupriavidus necator |  |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene H16_B2073, promoter determination, subcloning and expression in Escherichia coli strains JM109 and S17-1, expression of inactive yellow fluorescent protein-tagged mutant S190A, colocalization of the PhaZd1 fusions with PHB granules, expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli | Cupriavidus necator |
| gene H16_B2401, promoter determination, subcloning and expression in Escherichia coli strains JM109 and S17-1, expression of inactive C-terminally yellow fluorescent protein-tagged mutant S193A, no colocalization with PHB granules, expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli | Cupriavidus necator |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | deletion of phaZd1 without effect on enzyme activity | Cupriavidus necator |
| additional information | deletion of phaZd2 without effect on enzyme activity | Cupriavidus necator |
| S190A | site-directed mutagenesis, inactive mutant | Cupriavidus necator |
| S193A | site-directed mutagenesis, inactive mutant | Cupriavidus necator |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | activates up to 10 mM, inhibits above; activates up to 10 mM, inhibits above | Cupriavidus necator | |
| DTE | - |
Cupriavidus necator | |
| EDTA | activates alone, but inhibits in presence of divalent cations; activates alone, but inhibits in presence of divalent cations | Cupriavidus necator | |
| iodoacetamide | - |
Cupriavidus necator | |
| Mg2+ | activates up to 10 mM, inhibits above; activates up to 10 mM, inhibits above | Cupriavidus necator | |
| additional information | activation of PhaZd2 depolymerase activity by salts, but salts affect the activity of PhaZd2 with nPHB granules as substrate but have no significant influence on the hydrolysis of p-nitrophenyl esters such as p-nitrophenyl butyrate. Poor effect by DTT; activation of PhaZd2 depolymerase activity by salts, but salts affect the activity of PhaZd2 with nPHB granules as substrate but have no significant influence on the hydrolysis of p-nitrophenyl esters such as p-nitrophenylbutyrate. Poor effect by DTT | Cupriavidus necator | |
| PMSF | - |
Cupriavidus necator | |
| SDS | almost complete inhibition at 0.01% v/v; almost complete inhibition at 0.01% v/v | Cupriavidus necator | |
| Triton X-100 | almost complete inhibition at 0.01% v/v; almost complete inhibition at 0.01% v/v | Cupriavidus necator | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| intracellular | - |
Cupriavidus necator | 5622 | - |
| additional information | the enzyme is not detected in the PHB granule fraction | Cupriavidus necator | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | activates up to 10 mM, inhibits above | Cupriavidus necator | |
| K+ | activates | Cupriavidus necator | |
| Mg2+ | activates up to 10 mM, inhibits above | Cupriavidus necator | |
| additional information | activation of PhaZd2 depolymerase activity by salts, but salts affect the activity of PhaZd2 with nPHB granules as substrate but have no significant influence on the hydrolysis of p-nitrophenyl esters such as p-nitrophenylbutyrate | Cupriavidus necator | |
| additional information | slight activation of PhaZd2 depolymerase activity by salts, but salts affect the activity of PhaZd1 with nPHB granules as substrate but have no significant influence on the hydrolysis of p-nitrophenyl esters such as p-nitrophenylbutyrate | Cupriavidus necator |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 38400 | - |
x * 38400, about, sequence calculation | Cupriavidus necator |
| 39200 | - |
x * 39200, about, sequence calculation | Cupriavidus necator |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Cupriavidus necator | Q0JYJ1 | gene H16_B2401 | - |
| Cupriavidus necator | Q0JZG9 | gene H16_B2073 | - |
| Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 | Q0JYJ1 | gene H16_B2401 | - |
| Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 | Q0JZG9 | gene H16_B2073 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli by nicke affinity chromatography | Cupriavidus necator |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-nitrophenyl butyrate + H2O | - |
Cupriavidus necator | 4-nitrophenol + butyrate | - |
? | |
| 4-nitrophenyl butyrate + H2O | - |
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 | 4-nitrophenol + butyrate | - |
? | |
| poly(3-hydroxybutyrate) + H2O | - |
Cupriavidus necator | ? | - |
? | |
| poly(3-hydroxybutyrate) + H2O | - |
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 38400, about, sequence calculation | Cupriavidus necator |
| ? | x * 39200, about, sequence calculation | Cupriavidus necator |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PhaZ6 | - |
Cupriavidus necator |
| PhaZ7 | - |
Cupriavidus necator |
| PhaZd1 | - |
Cupriavidus necator |
| PhaZd2 | - |
Cupriavidus necator |
| PHB depolymerase | - |
Cupriavidus necator |
| poly(3-hydroxybutyrate) depolymerase | - |
Cupriavidus necator |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
assay at | Cupriavidus necator |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | chromosomal deletion of phaZd1, phaZd2, or both depolymerase genes has no significant effect on PHB accumulation and mobilization during growth in nutrient broth or nutrient broth-gluconate medium | Cupriavidus necator |
| additional information | active site Ser190 | Cupriavidus necator |
| additional information | active site Ser193 | Cupriavidus necator |
| physiological function | PhaZd1 and is a poly(3-hydroxybutyrate) depolymerase with a high capacity to degrade poly(3-hydroxybutyrate) when artificially expressed but is apparently not involved in poly(3-hydroxybutyrate) mobilization in the wild-type. But constitutive expression of PhaZd1 reduces or even prevents the accumulation of poly(3-hydroxybutyrate) under poly(3-hydroxybutyrate)-permissive conditions in vivo | Cupriavidus necator |
| physiological function | PhaZd1 and is a poly(3-hydroxybutyrate) depolymerase with a high capacity to degrade poly(3-hydroxybutyrate) when artificially expressed but is apparently not involved in poly(3-hydroxybutyrate) mobilization in the wild-type. But constitutive expression of PhaZd2 reduces or even prevents the accumulation of poly(3-hydroxybutyrate) under poly(3-hydroxybutyrate)-permissive conditions in vivo | Cupriavidus necator |
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