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Literature summary extracted from

  • Yu, P.; Wang, X.T.; Liu, J.W.
    Purification and characterization of a novel cold-adapted phytase from Rhodotorula mucilaginosa strain JMUY14 isolated from Antarctic (2015), J. Basic Microbiol., 55, 1029-1039 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.3.8 EDTA
-
Rhodotorula mucilaginosa
3.1.3.8 EGTA
-
Rhodotorula mucilaginosa
3.1.3.26 EDTA
-
Rhodotorula mucilaginosa
3.1.3.26 EGTA
-
Rhodotorula mucilaginosa

Application

EC Number Application Comment Organism
3.1.3.8 agriculture supplementation of phytases into the monogastric animals feed can reduce the phosphorus excretion and result in improved availability of trace elements, minerals, amino acids, and energy. The enzyme has great potential for feed applications, especially in aquaculture Rhodotorula mucilaginosa
3.1.3.8 nutrition due to its specific enzymatic activity, phytase is considered a green feed additive, which can effectively improve the availability of phytate-P and, simultaneously, eliminate the anti-nutritional function of phytate, resulting in a lower production cost and improved environmental protection Rhodotorula mucilaginosa
3.1.3.26 agriculture supplementation of phytases into the monogastric animals feed can reduce the phosphorus excretion and result in improved availability of trace elements, minerals, amino acids, and energy. The enzyme has great potential for feed applications, especially in aquaculture Rhodotorula mucilaginosa
3.1.3.26 nutrition due to its specific enzymatic activity, phytase is considered a green feed additive, which can effectively improve the availability of phytate-P and, simultaneously, eliminate the anti-nutritional function of phytate, resulting in a lower production cost and improved environmental protection Rhodotorula mucilaginosa

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.8 phylogenetic tree Rhodotorula mucilaginosa
3.1.3.26 phylogenetic tree Rhodotorula mucilaginosa

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.8 Ag+
-
Rhodotorula mucilaginosa
3.1.3.8 Cu2+
-
Rhodotorula mucilaginosa
3.1.3.8 Mn2+
-
Rhodotorula mucilaginosa
3.1.3.8 additional information the enzyme shows strong protease resistance, after being incubated with 0.1 mg/ml of pepsin and trypsin at 37°C for 1 h, the residual activity is 92.2% and 75.6%, respectively Rhodotorula mucilaginosa
3.1.3.8 phenylglyoxal hydrate
-
Rhodotorula mucilaginosa
3.1.3.8 PMSF
-
Rhodotorula mucilaginosa
3.1.3.8 SDS
-
Rhodotorula mucilaginosa
3.1.3.8 Zn2+
-
Rhodotorula mucilaginosa
3.1.3.26 Ag+
-
Rhodotorula mucilaginosa
3.1.3.26 Cu2+
-
Rhodotorula mucilaginosa
3.1.3.26 Mn2+
-
Rhodotorula mucilaginosa
3.1.3.26 additional information the enzyme shows strong protease resistance, after being incubated with 0.1 mg/ml of pepsin and trypsin at 37°C for 1 h, the residual activity is 92.2% and 75.6%, respectively Rhodotorula mucilaginosa
3.1.3.26 phenylglyoxal hydrate
-
Rhodotorula mucilaginosa
3.1.3.26 PMSF
-
Rhodotorula mucilaginosa
3.1.3.26 SDS
-
Rhodotorula mucilaginosa
3.1.3.26 Zn2+
-
Rhodotorula mucilaginosa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.8 additional information
-
additional information Lineweaver-Burk plots Rhodotorula mucilaginosa
3.1.3.8 0.247
-
myo-inositol hexakisphosphate pH 5.0, 37°C Rhodotorula mucilaginosa
3.1.3.26 additional information
-
additional information Lineweaver-Burk plots Rhodotorula mucilaginosa
3.1.3.26 0.247
-
myo-inositol hexakisphosphate pH 5.0, 37°C Rhodotorula mucilaginosa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.3.8 extracellular the enzyme is secreted Rhodotorula mucilaginosa
-
-
3.1.3.26 extracellular the enzyme is secreted Rhodotorula mucilaginosa
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.8 Ca2+ activates Rhodotorula mucilaginosa
3.1.3.8 Fe2+ activates Rhodotorula mucilaginosa
3.1.3.8 Fe3+ activates Rhodotorula mucilaginosa
3.1.3.8 K+ activates Rhodotorula mucilaginosa
3.1.3.8 Mg2+ activates Rhodotorula mucilaginosa
3.1.3.8 Na+ activates Rhodotorula mucilaginosa
3.1.3.26 Ca2+ activates Rhodotorula mucilaginosa
3.1.3.26 Fe2+ activates Rhodotorula mucilaginosa
3.1.3.26 Fe3+ activates Rhodotorula mucilaginosa
3.1.3.26 K+ activates Rhodotorula mucilaginosa
3.1.3.26 Mg2+ activates Rhodotorula mucilaginosa
3.1.3.26 Na+ activates Rhodotorula mucilaginosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.3.8 myo-inositol hexakisphosphate + H2O Rhodotorula mucilaginosa phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 1D-myo-inositol pentakisphosphate + phosphate
-
?
3.1.3.8 myo-inositol hexakisphosphate + H2O Rhodotorula mucilaginosa JMUY14 phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 1D-myo-inositol pentakisphosphate + phosphate
-
?
3.1.3.26 myo-inositol hexakisphosphate + H2O Rhodotorula mucilaginosa phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 1D-myo-inositol pentakisphosphate + phosphate
-
?
3.1.3.26 myo-inositol hexakisphosphate + H2O Rhodotorula mucilaginosa JMUY14 phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 1D-myo-inositol pentakisphosphate + phosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.8 Rhodotorula mucilaginosa
-
isolated from Antarctic deep-sea sediment
-
3.1.3.8 Rhodotorula mucilaginosa JMUY14
-
isolated from Antarctic deep-sea sediment
-
3.1.3.26 Rhodotorula mucilaginosa
-
isolated from Antarctic deep-sea sediment
-
3.1.3.26 Rhodotorula mucilaginosa JMUY14
-
isolated from Antarctic deep-sea sediment
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.8 native extracellular enzyme 15.2fold by ammonium sulfate fractionation, anion and cation exchange chromatography, and gel filtration, to homogeneity Rhodotorula mucilaginosa
3.1.3.26 native extracellular enzyme 15.2fold by ammonium sulfate fractionation, anion and cation exchange chromatography, and gel filtration, to homogeneity Rhodotorula mucilaginosa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.8 cell culture fermentation is optimized by a response surface methodology based on the Box-Behnken design, production leads to maximum activity of phytase of 205.45 U/ml Rhodotorula mucilaginosa
-
3.1.3.26 cell culture fermentation is optimized by a response surface methodology based on the Box-Behnken design, production leads to maximum activity of phytase of 205.45 U/ml Rhodotorula mucilaginosa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.3.8 36.26
-
crude enzyme, pH 5.0, 37°C Rhodotorula mucilaginosa
3.1.3.26 36.26
-
crude enzyme, pH 5.0, 37°C Rhodotorula mucilaginosa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.8 additional information color reagents, containing 33.3% v/v nitric acid, 10% w/v ammonium molybdate, and 0.24% w/v ammonium vanadate v/v in a 2:1:1 ratio, for stop of enzyme reaction and product determination Rhodotorula mucilaginosa ?
-
?
3.1.3.8 additional information color reagents, containing 33.3% v/v nitric acid, 10% w/v ammonium molybdate, and 0.24% w/v ammonium vanadate v/v in a 2:1:1 ratio, for stop of enzyme reaction and product determination Rhodotorula mucilaginosa JMUY14 ?
-
?
3.1.3.8 myo-inositol hexakisphosphate + H2O phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 Rhodotorula mucilaginosa 1D-myo-inositol pentakisphosphate + phosphate
-
?
3.1.3.8 myo-inositol hexakisphosphate + H2O substrate is sodium phytate or calcium phytate, phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 Rhodotorula mucilaginosa 1D-myo-inositol pentakisphosphate + phosphate
-
?
3.1.3.8 myo-inositol hexakisphosphate + H2O phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 Rhodotorula mucilaginosa JMUY14 1D-myo-inositol pentakisphosphate + phosphate
-
?
3.1.3.26 additional information color reagents, containing 33.3% v/v nitric acid, 10% w/v ammonium molybdate, and 0.24% w/v ammonium vanadate v/v in a 2:1:1 ratio, for stop of enzyme reaction and product determination Rhodotorula mucilaginosa ?
-
?
3.1.3.26 additional information color reagents, containing 33.3% v/v nitric acid, 10% w/v ammonium molybdate, and 0.24% w/v ammonium vanadate v/v in a 2:1:1 ratio, for stop of enzyme reaction and product determination Rhodotorula mucilaginosa JMUY14 ?
-
?
3.1.3.26 myo-inositol hexakisphosphate + H2O phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 Rhodotorula mucilaginosa 1D-myo-inositol pentakisphosphate + phosphate
-
?
3.1.3.26 myo-inositol hexakisphosphate + H2O substrate is sodium phytate or calcium phytate, phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 Rhodotorula mucilaginosa 1D-myo-inositol pentakisphosphate + phosphate
-
?
3.1.3.26 myo-inositol hexakisphosphate + H2O phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 Rhodotorula mucilaginosa JMUY14 1D-myo-inositol pentakisphosphate + phosphate
-
?
3.1.3.26 myo-inositol hexakisphosphate + H2O substrate is sodium phytate or calcium phytate, phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 Rhodotorula mucilaginosa JMUY14 1D-myo-inositol pentakisphosphate + phosphate
-
?

Subunits

EC Number Subunits Comment Organism
3.1.3.8 ? x * 63000, about, sequence calculation Rhodotorula mucilaginosa
3.1.3.26 ? x * 63000, about, sequence calculation Rhodotorula mucilaginosa

Synonyms

EC Number Synonyms Comment Organism
3.1.3.8 More cf. EC 3.1.3.26 Rhodotorula mucilaginosa
3.1.3.8 myo-inositol hexakisphosphate phosphohydrolase
-
Rhodotorula mucilaginosa
3.1.3.26 More cf. EC 3.1.3.8 Rhodotorula mucilaginosa
3.1.3.26 myo-inositol hexakisphosphate phosphohydrolase
-
Rhodotorula mucilaginosa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.8 50
-
-
Rhodotorula mucilaginosa
3.1.3.26 50
-
-
Rhodotorula mucilaginosa

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.3.8 additional information
-
a cold-adapted phytase Rhodotorula mucilaginosa
3.1.3.8 25 55 over 50% of maximal activity within this range, maximal activity at 50°C, inactive at 60°C Rhodotorula mucilaginosa
3.1.3.26 additional information
-
a cold-adapted phytase Rhodotorula mucilaginosa
3.1.3.26 25 55 over 50% of maximal activity within this range, maximal activity at 50°C, inactive at 60°C Rhodotorula mucilaginosa

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.3.8 50 75 the purified phytase retains 73.6% of its activity after being incubated at 50°C for 10 min, while its activity is quickly lost after incubation at 65°C or 70°C for 10 min Rhodotorula mucilaginosa
3.1.3.26 50 75 the purified phytase retains 73.6% of its activity after being incubated at 50°C for 10 min, while its activity is quickly lost after incubation at 65°C or 70°C for 10 min Rhodotorula mucilaginosa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.8 5
-
-
Rhodotorula mucilaginosa
3.1.3.26 5
-
-
Rhodotorula mucilaginosa

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.3.8 3 5.5 optimum pH 5.0, over 80% of maximal activity at pH 3.0-5.5, dramatical loss of activity above pH 5.5 Rhodotorula mucilaginosa
3.1.3.26 3 5.5 optimum pH 5.0, over 80% of maximal activity at pH 3.0-5.5, dramatical loss of activity above pH 5.5 Rhodotorula mucilaginosa

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.3.8 3 7 purified native enzyme is quite stable in this range Rhodotorula mucilaginosa
3.1.3.26 3 7 purified native enzyme is quite stable in this range Rhodotorula mucilaginosa

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.1.3.8 Rhodotorula mucilaginosa sequence calculation
-
4.33
3.1.3.26 Rhodotorula mucilaginosa sequence calculation
-
4.33