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Literature summary for 3.4.13.19 extracted from
- Characterization of a Bifidobacterium longum BORI dipeptidase belonging to the U34 family (2007), Appl. Environ. Microbiol., 73, 5598-5606.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli | Bifidobacterium longum |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 49000 | - |
native enzyme, SDS-PAGE | Bifidobacterium longum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bifidobacterium longum | - |
- |
- |
| Bifidobacterium longum BORI | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme is purified by nickel-chelating affinity chromatography, wild type enzyme is purified by ammonium sulfate precipitation, DEAE-cellulose column chromatography, and Q-Sepharose column chromatography | Bifidobacterium longum |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
0.71 units/mg from cell extract, 77.2 units/mg after 109fold purification, one unit is defined as that required to increase the absorbance by one unit per minute | Bifidobacterium longum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Ala-Ala + H2O | 62.5% activity compared to Ala-Gln | Bifidobacterium longum | Ala + Ala | - |
? |  |
| Ala-Ala + H2O | 62.5% activity compared to Ala-Gln | Bifidobacterium longum BORI | Ala + Ala | - |
? | |
| Ala-Gln + H2O | 100% activity | Bifidobacterium longum | Ala + Gln | - |
? | |
| Ala-Gly + H2O | 68.9% activity compared to Ala-Gln | Bifidobacterium longum | Ala + Gly | - |
? | |
| Ala-Gly + H2O | 68.9% activity compared to Ala-Gln | Bifidobacterium longum BORI | Ala + Gly | - |
? | |
| Ala-Leu + H2O | 14.0% activity compared to Ala-Gln | Bifidobacterium longum | Ala + Leu | - |
? | |
| Ala-Phe + H2O | 14.0% activity compared to Ala-Gln | Bifidobacterium longum | Ala + Phe | - |
? | |
| Ala-Phe + H2O | 14.0% activity compared to Ala-Gln | Bifidobacterium longum BORI | Ala + Phe | - |
? | |
| Arg-Phe + H2O | 6.3% activity compared to Ala-Gln | Bifidobacterium longum | Arg + Phe | - |
? | |
| Asp-Phe + H2O | 4.9% activity compared to Ala-Gln | Bifidobacterium longum | Asp + Phe | - |
? | |
| Leu-Leu + H2O | 71% activity compared to Ala-Gln | Bifidobacterium longum | Leu + Leu | - |
? | |
| Leu-Phe + H2O | 12.5% activity compared to Ala-Gln | Bifidobacterium longum | Leu + Phe | - |
? | |
| Leu-Trp + H2O | 10.2% activity compared to Ala-Gln | Bifidobacterium longum | Leu + Trp | - |
? | |
| additional information | low activity toward dipeptides containing aromatic amino acids except for Phe-Gly, does not hydrolyze Leu-Asp, Phe-Phe, or N- or C-terminus-blocked dipeptides (N-carbobenzyloxy-Phe-Gly, N-carbobenzyloxy-Ala-Leu, or Leu-Leu-amide), does not hydrolyze tri-, tetra-, or pentapeptides or p-nitroanilide derivatives of dipeptides and peptides | Bifidobacterium longum | ? | - |
? | |
| additional information | low activity toward dipeptides containing aromatic amino acids except for Phe-Gly, does not hydrolyze Leu-Asp, Phe-Phe, or N- or C-terminus-blocked dipeptides (N-carbobenzyloxy-Phe-Gly, N-carbobenzyloxy-Ala-Leu, or Leu-Leu-amide), does not hydrolyze tri-, tetra-, or pentapeptides or p-nitroanilide derivatives of dipeptides and peptides | Bifidobacterium longum BORI | ? | - |
? | |
| Phe-Ala + H2O | 6.7% activity compared to Ala-Gln | Bifidobacterium longum | Phe + Ala | - |
? | |
| Phe-Gly + H2O | 74.1% activity compared to Ala-Gln | Bifidobacterium longum | Phe + Gly | - |
? | |
| Phe-Gly + H2O | 74.1% activity compared to Ala-Gln | Bifidobacterium longum BORI | Phe + Gly | - |
? | |
| Tyr-Leu + H2O | 9.5% activity compared to Ala-Gln | Bifidobacterium longum | Tyr + Leu | - |
? | |
| Tyr-Phe + H2O | 3.8% activity compared to Ala-Gln | Bifidobacterium longum | Tyr + Phe | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| dipeptidase | capable of hydrolyzing a range of dipeptides but not tri- and tetrapeptides, p-nitroanilide derivatives of amino acids, or N- or C-terminus-blocked dipeptides | Bifidobacterium longum |
| PepD | - |
Bifidobacterium longum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
- |
Bifidobacterium longum |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | 60 | - |
Bifidobacterium longum |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 70 | the enzyme shows about 30% and 50% of the maximum activity at 20°C and 70°C, respectively, stable at temperatures up to 70°C, but the activity decreased rapidly above 80°C | Bifidobacterium longum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
- |
Bifidobacterium longum |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 9 | - |
Bifidobacterium longum |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 10 | very low activity (less than about 10%) is observed below pH 5.5, at pH 10.0 the activity is about 50% of the maximum, the enzyme is stable for 30 min over the pH range 4.0 to 8.0 | Bifidobacterium longum |
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