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Literature summary for 4.1.2.52 extracted from
- Purification and biochemical characterization of a pyruvate-specific class II aldolase, HpaI (2005), Biochemistry, 44, 9447-9455.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| HpaI wild type and R70A mutant expressed in Escherichia coli BL21(lambda DE3) under the control of the T7 promoter from expression plasmid pT7-7 | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| R70A | replacement by site-specific mutagenesis results in an enzyme that lacks both aldolase and decarboxylase activities. The mutant enzyme is also unable to catalyze pyruvate proton exchange | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| pyruvate | - |
Escherichia coli |  |
| sodium oxalate | - |
Escherichia coli | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.006 | - |
4-hydroxy-2-oxopentanoate | Km (app) with Co2+, pH 8.0, 25°C | Escherichia coli | |
| 0.0175 | - |
4-hydroxy-2-oxopentanoate | Km (app) with Mn2+, pH 8.0, 25°C | Escherichia coli | |
| 0.16 | - |
4-hydroxy-2-oxohexanoate | pH 8.0, 25°C | Escherichia coli | |
| 0.289 | - |
4-hydroxy-2-oxopentanoate | Km (app) with Mg2+, pH 8.0, 25°C | Escherichia coli | |
| 0.38 | - |
4-hydroxy-2-oxopentanoate | pH 8.0, 25°C | Escherichia coli | |
| 14.22 | - |
3-deoxy-D-manno-oct-2-ulosonic acid | i.e. KDO, pH 8.0, 25°C | Escherichia coli | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Cd2+ | 0.5 mM chloride salt, 4% relative activity, with 4-hydroxy-2-oxopentanoate as substrate | Escherichia coli | |
| Co2+ | 0.5 mM chloride salt, 100% relative activity, with 4-hydroxy-2-oxopentanoate as substrate | Escherichia coli | |
| Cu2+ | 0.5 mM chloride salt, 1% relative activity, with 4-hydroxy-2-oxopentanoate as substrate | Escherichia coli | |
| Fe2+ | 0.5 mM chloride salt, 57% relative activity, with 4-hydroxy-2-oxopentanoate as substrate | Escherichia coli | |
| Mg2+ | 0.5 mM chloride salt, 49% relative activity, with 4-hydroxy-2-oxopentanoate as substrate | Escherichia coli | |
| Mn2+ | 0.5 mM chloride salt, 99% relative activity, with 4-hydroxy-2-oxopentanoate as substrate | Escherichia coli | |
| additional information | no activity with Ca2+, Fe3+, Cr3+ and Al3+ | Escherichia coli | |
| Ni2+ | 0.5 mM chloride salt, 11% relative activity, with 4-hydroxy-2-oxopentanoate as substrate | Escherichia coli | |
| Zn2+ | 0.5 mM chloride salt, 73% relative activity, with 4-hydroxy-2-oxopentanoate as substrate | Escherichia coli | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 28000 | - |
subunit, SDS-PAGE | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-hydroxy-2-oxoheptanedioate | Escherichia coli | - |
pyruvate + succinate semialdehyde | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | Q47098 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| wild type protein and R70A mutant protein purified to homogeneity using anion exchange, hydrophobic interaction, and gel filtration chormatography | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-deoxy-D-manno-oct-2-ulosonic acid | 3-deoxy-D-manno-oct-2-ulosonic acid i.e. KDO | Escherichia coli | ? | - |
? | |
| 4-hydroxy-2-oxoheptanedioate | - |
Escherichia coli | pyruvate + succinate semialdehyde | - |
? | |
| 4-hydroxy-2-oxohexanoate | - |
Escherichia coli | ? | - |
? | |
| 4-hydroxy-2-oxopentanoate | - |
Escherichia coli | ? | - |
? | |
| additional information | the enzyme exhibits significant oxaloacetate decarboxylase activity, with a kcat value 2.4fold higher than the corresponding value for the aldol cleavage of 4-hydroxy-2-oxopentanoate | Escherichia coli | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| HpaI | - |
Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.55 | - |
3-deoxy-D-manno-oct-2-ulosonic acid | i.e. KDO, pH 8.0, 25°C | Escherichia coli | |
| 229 | - |
4-hydroxy-2-oxohexanoate | pH 8.0, 25°C | Escherichia coli | |
| 353 | - |
4-hydroxy-2-oxopentanoate | pH 8.0, 25°C | Escherichia coli | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0055 | - |
sodium oxalate | pH 8.0, 25°C | Escherichia coli | |
| 0.53 | - |
pyruvate | pH 8.0, 25°C | Escherichia coli | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | enzyme is involved in the catabolic pathway of hydroxyphenylacetate | Escherichia coli |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.03868 | - |
3-deoxy-D-manno-oct-2-ulosonic acid | i.e. KDO, pH 8.0, 25°C | Escherichia coli | |
| 940 | - |
4-hydroxy-2-oxopentanoate | pH 8.0, 25°C | Escherichia coli | |
| 1460 | - |
4-hydroxy-2-oxohexanoate | pH 8.0, 25°C | Escherichia coli | |
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