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Literature summary extracted from

  • Yamamoto, Y.; Kawashima, D.; Hashizume, A.; Hisamatsu, M.; Isono, N.
    Purification and characterization of 1,3-beta-D-glucan phosphorylase from Ochromonas danica (2013), Biosci. Biotechnol. Biochem., 77, 1949-1954.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.97 4.1
-
 laminaritriose with phosphate, pH 7.5, 30°C Ochromonas danica
2.4.1.97 4.4
-
 phosphate with laminaritriose, pH 7.5, 30°C Ochromonas danica

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.1.97 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
2.4.1.97 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
2.4.1.97 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
2.4.1.97 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
2.4.1.97 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
2.4.1.97 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
2.4.1.97 250000
-
 by gel filtration, indicating a homodimer and/or a heterodimer Ochromonas danica

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.97 Ochromonas danica
-
 belongs to the class Chrysophyceae, golden algae
-
2.4.1.97 Ochromonas danica NIES-2142
-
 belongs to the class Chrysophyceae, golden algae
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.97 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

EC Number Reaction Comment Organism Reaction ID
2.4.1.97 [(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
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.1.97 26.5
-
 purified enzyme, 30°C, pH 7.5 Ochromonas danica

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.97 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
2.4.1.97 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
2.4.1.97 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
2.4.1.97 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
2.4.1.97 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
2.4.1.97 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
2.4.1.97 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
2.4.1.97 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
2.4.1.97 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 ?
-
 ?
2.4.1.97 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

EC Number Subunits Comment Organism
2.4.1.97 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
2.4.1.97 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

EC Number Synonyms Comment Organism
2.4.1.97 Bgp
-
 Ochromonas danica
2.4.1.97 OdBGP
-
 Ochromonas danica

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.97 25 30 assay at 30°C Ochromonas danica

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.4.1.97 40
-
 stable up to 40°C at pH 7.5 for 30 min Ochromonas danica

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.4.1.97 400
-
 laminaritriose with phosphate, pH 7.5, 30°C Ochromonas danica

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.97 5.5
-
 the activity is low at neutral pH and almost no activity is observed at pH 8.5 Ochromonas danica
2.4.1.97 7.5
-
 assay at Ochromonas danica

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.4.1.97 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

EC Number pH Stability pH Stability Maximum Comment Organism
2.4.1.97 4.7 9.1 at 4°C for 15 h Ochromonas danica