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Literature summary for 4.1.1.17 extracted from
- Characterization of the Entamoeba histolytica ornithine decarboxylase-like enzyme (2008), PLoS Negl. Trop. Dis., 2, e115.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| ODC is encoded by a single-copy gene located on a 1900 kb chromosome, DNA and amino acid sequence determination and analysis, phylogenetic tree, overexpression of the His- and S-tagged enzyme in Escherichia coli | Entamoeba histolytica |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | the wild-type enzyme's substrate binding site is mutated at three amino acids D332, D361, and Y323 leading to reduced substrate binding activity, computational modelling, overview | Entamoeba histolytica |
General Stability
| General Stability | Organism |
|---|---|
| dithiothreitol stabilizes the enzyme | Entamoeba histolytica |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | no inhibition of the Entamoeba histolytica enzyme by specific irreversible ODC inhibitor alpha-difluoromethylornithine, DFMO, the recombinant enzyme shows altered amino acid sequence and three-dimensional structure, Entamoeba histolytica putative ODC has a putative binding site for DFMO with substituted disrupted amino acids D332, D361, and Y323 by H296, F305, and N334, through which this inhibitor interacts with the protein | Entamoeba histolytica |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 46000 | - |
x * 46000, about, sequence calculation, x * 48000, recombinant His- and S-tagged enzyme, SDS-PAGE | Entamoeba histolytica |
| 48000 | - |
x * 46000, about, sequence calculation, x * 48000, recombinant His- and S-tagged enzyme, SDS-PAGE | Entamoeba histolytica |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-ornithine | Entamoeba histolytica | ornithine decarboxylase, the first and rate-limiting enzyme in the polyamine biosynthetic pathway, is a highly regulated enzyme | putrescine + CO2 | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Entamoeba histolytica | Q58P26 | clone 6 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His- and S-tagged enzyme from Escherichia coli by nickel affinity chromatography | Entamoeba histolytica |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.0219 | - |
purified recombinant enzyme | Entamoeba histolytica |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-ornithine | ornithine decarboxylase, the first and rate-limiting enzyme in the polyamine biosynthetic pathway, is a highly regulated enzyme | Entamoeba histolytica | putrescine + CO2 | - |
? | |
| L-ornithine | the wild-type enzyme's substrate binding site is mutated at three amino acids D332, D361, and Y323 leading to reduced substrate binding activity, computational modelling, overview | Entamoeba histolytica | putrescine + CO2 | - |
? | |
| additional information | no activity using arginine and lysine as substrates | Entamoeba histolytica | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 46000, about, sequence calculation, x * 48000, recombinant His- and S-tagged enzyme, SDS-PAGE | Entamoeba histolytica |
| More | structural analysis and modelling | Entamoeba histolytica |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ODC | - |
Entamoeba histolytica |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Entamoeba histolytica |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Entamoeba histolytica |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | bindig site structure, modelling | Entamoeba histolytica | |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Entamoeba histolytica | sequence calculation | - |
5.61 |
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