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Literature summary for 2.4.1.97 extracted from
- Purification and characterization of 1,3-beta-D-glucan phosphorylase from Ochromonas danica (2013), Biosci. Biotechnol. Biochem., 77, 1949-1954.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 4.1 | - |
laminaritriose | with phosphate, pH 7.5, 30°C | Ochromonas danica |  |
| 4.4 | - |
phosphate | with laminaritriose, pH 7.5, 30°C | Ochromonas danica | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 113000 | - |
x * 113000, x * 118000, x * 124000, and/or heterodimer, native enzyme 250000 Da, SDS-PAGE, the three bands can not be separated | Ochromonas danica |
| 113000 | - |
x * 113000, x * 118000, x * 124000, and/or homodimer, native enzyme 250000 Da, SDS-PAGE, the three bands can not be separated | Ochromonas danica |
| 118000 | - |
x * 113000, x * 118000, x * 124000, and/or heterodimer, native enzyme 250000 Da, SDS-PAGE, the three bands can not be separated | Ochromonas danica |
| 118000 | - |
x * 113000, x * 118000, x * 124000, and/or homodimer, native enzyme 250000 Da, SDS-PAGE, the three bands can not be separated | Ochromonas danica |
| 124000 | - |
x * 113000, x * 118000, x * 124000, and/or heterodimer, native enzyme 250000 Da, SDS-PAGE, the three bands can not be separated | Ochromonas danica |
| 124000 | - |
x * 113000, x * 118000, x * 124000, and/or homodimer, native enzyme 250000 Da, SDS-PAGE, the three bands can not be separated | Ochromonas danica |
| 250000 | - |
by gel filtration, indicating a homodimer and/or a heterodimer | Ochromonas danica |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Ochromonas danica | - |
belongs to the class Chrysophyceae, golden algae | - |
| Ochromonas danica NIES-2142 | - |
belongs to the class Chrysophyceae, golden algae | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| purified from a cell-free extract by ammonium sulfate fractionation and 3 steps of column chromatography, 93.3 fold with a yield 16.7%, 2 mg of purified enzyme is obtained from 5 l culture | Ochromonas danica |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| [(1->3)-beta-D-glucosyl]n + phosphate = [(1->3)-beta-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate | the enzyme also synthesizes 1,3-beta-glucan from alpha-D-glucose 1-phosphate and laminaribiose. Kinetic analysis indicate a sequential bi bi reaction mechanism | Ochromonas danica |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 26.5 | - |
purified enzyme, 30°C, pH 7.5 | Ochromonas danica |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| laminarihexaose + phosphate | the enzyme can catalyze reactions in both synthetic and phosphorolytic directions. Equilibrium studies indicate that the enzyme favors the reaction in the synthetic direction | Ochromonas danica | laminaripentaose + alpha-D-glucose 1-phosphate | - |
r | |
| laminarihexaose + phosphate | the enzyme can catalyze reactions in both synthetic and phosphorolytic directions. Equilibrium studies indicate that the enzyme favors the reaction in the synthetic direction | Ochromonas danica NIES-2142 | laminaripentaose + alpha-D-glucose 1-phosphate | - |
r | |
| laminaripentaose + phosphate | the enzyme can catalyze reactions in both synthetic and phosphorolytic directions. Equilibrium studies indicate that the enzyme favors the reaction in the synthetic direction | Ochromonas danica | laminaritetraose + alpha-D-glucose 1-phosphate | - |
r | |
| laminaripentaose + phosphate | the enzyme can catalyze reactions in both synthetic and phosphorolytic directions. Equilibrium studies indicate that the enzyme favors the reaction in the synthetic direction | Ochromonas danica NIES-2142 | laminaritetraose + alpha-D-glucose 1-phosphate | - |
r | |
| laminaritetraose + phosphate | the enzyme can catalyze reactions in both synthetic and phosphorolytic directions. Equilibrium studies indicate that the enzyme favors the reaction in the synthetic direction | Ochromonas danica | laminaritriose + alpha-D-glucose 1-phosphate | - |
r | |
| laminaritetraose + phosphate | the enzyme can catalyze reactions in both synthetic and phosphorolytic directions. Equilibrium studies indicate that the enzyme favors the reaction in the synthetic direction | Ochromonas danica NIES-2142 | laminaritriose + alpha-D-glucose 1-phosphate | - |
r | |
| laminaritriose + phosphate | the enzyme can catalyze reactions in both synthetic and phosphorolytic directions. Equilibrium studies indicate that the enzyme favors the reaction in the synthetic direction | Ochromonas danica | laminaribiose + alpha-D-glucose 1-phosphate | products analysed by thin layer chromatography TLC | r | |
| laminaritriose + phosphate | the enzyme can catalyze reactions in both synthetic and phosphorolytic directions. Equilibrium studies indicate that the enzyme favors the reaction in the synthetic direction | Ochromonas danica NIES-2142 | laminaribiose + alpha-D-glucose 1-phosphate | products analysed by thin layer chromatography TLC | r | |
| additional information | no phosphorolytic reaction with glucose, laminaribiose, cellobiose, celltriose, cellotetraose, cellopentaose, sohorose, gentiobiose, trehalose, kojibiose, nigerise, maltose, isomaltose, methyl alpha-D-glucopyranoside, methyl beta-D-glucopyranoside, p-nitrophenyl alpha-D-glucopyranoside, and p-nitrophenyl beta-D-glucopyranoside | Ochromonas danica | ? | - |
? | |
| additional information | no phosphorolytic reaction with glucose, laminaribiose, cellobiose, celltriose, cellotetraose, cellopentaose, sohorose, gentiobiose, trehalose, kojibiose, nigerise, maltose, isomaltose, methyl alpha-D-glucopyranoside, methyl beta-D-glucopyranoside, p-nitrophenyl alpha-D-glucopyranoside, and p-nitrophenyl beta-D-glucopyranoside | Ochromonas danica NIES-2142 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterodimer | x * 113000, x * 118000, x * 124000, and/or homodimer, native enzyme 250000 Da, SDS-PAGE, the three bands can not be separated | Ochromonas danica |
| homodimer | x * 113000, x * 118000, x * 124000, and/or heterodimer, native enzyme 250000 Da, SDS-PAGE, the three bands can not be separated | Ochromonas danica |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Bgp | - |
Ochromonas danica |
| OdBGP | - |
Ochromonas danica |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 30 | assay at 30°C | Ochromonas danica |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
stable up to 40°C at pH 7.5 for 30 min | Ochromonas danica |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 400 | - |
laminaritriose | with phosphate, pH 7.5, 30°C | Ochromonas danica | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | - |
the activity is low at neutral pH and almost no activity is observed at pH 8.5 | Ochromonas danica |
| 7.5 | - |
assay at | Ochromonas danica |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
optimum at pH 5.5, the activity is low at neutral pH and almost no activity is observed at pH 8.5 | Ochromonas danica |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 4.7 | 9.1 | at 4°C for 15 h | Ochromonas danica |
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