Literature summary for 4.6.1.24 extracted from

Kobayashi, H.; Katsutani, T.; Hara, Y.; Motoyoshi, N.; Itagaki, T.; Akita, F.; Higashiura, A.; Yamada, Y.; Inokuchi, N.; Suzuki, M.
X-ray crystallographic structure of RNase Po1 that exhibits anti-tumor activity (2014), Biol. Pharm. Bull., 37, 968-978.

Search for more literature for 4.6.1.24

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant enzyme expression in Escherichia coli strain BL21(DE3) pLysS	Pleurotus ostreatus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme, hanging drop vapor diffusion method, mixing of 500 nl of 10 mg/mL protein in 20 mM Tris-HCl, pH 7.5, with 500 nl of reservoir solution containing 4 M sodium formate, 0.1 M Bis-Tris propane, pH 7.0, 10% PEG 400, and 300 nl 2 M caesium chloride, 20°C, 3 days, X-ray diffraction structure determination and analysis at 1.85 A resolution, molecular replacement method	Pleurotus ostreatus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
additional information	RNase Po1 might bind to the plasma membrane electrostatically	Pleurotus ostreatus	-	-

Organism

Organism	UniProt	Comment	Textmining
Pleurotus ostreatus	P81762	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme from Escherichia coli strain BL21(DE3)pLysS to homogeneity by ammonium sulfate fractionation, gel filtration, cation exchange and anion exchange chromatography, and again gel filtration, heparin affinity chromatography, and dialysis	Pleurotus ostreatus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme is a guanylic acid-specific ribonuclease	Pleurotus ostreatus	?	-	?

Subunits

Subunits	Comment	Organism
More	comparison of primary, secondary, and tertiary structures of RNase Po1 and RNase T1, overview	Pleurotus ostreatus

Synonyms

Synonyms	Comment	Organism
RNase Po1	-	Pleurotus ostreatus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Pleurotus ostreatus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	-	Pleurotus ostreatus

General Information

General Information	Comment	Organism
evolution	the enzyme belongs to the RNase T1 family, comparison of the amino acid sequences, overview	Pleurotus ostreatus
additional information	comparison of the electrostatic potential of the molecular surfaces of RNase Po1 and RNase T1 shows that RNase T1 is anionic whereas RNase Po1 is cationic, so RNase Po1 might bind to the plasma membrane electrostatically, determination of the three-dimensional X-ray structure of RNase Po1 and comparison to that of RNase T1. One of the additional disulfide bond is in the catalytic and binding site of RNase Po1, and makes RNase Po1 more stable than RNase T1. The base recognition site of RNase T1 consists of Tyr42, Asn43, Asn44, Glu46, Tyr45, and Asn98 and is located in the loop between beta3-4 strands (Asn43, Asn44, Tyr45, Glu46) and in the loop between beta6-7 strands (Asn98). In case of the base recognition site of RNase Po1, the amino acid residues Tyr38, Asn39, Asn40, Phe41, Glu42, and Asn94 correspond to those of RNase T1	Pleurotus ostreatus
physiological function	the enzyme is cytotoxic and inhibits the proliferation of human tumor cells, the enzyme is internalized into tumour cells	Pleurotus ostreatus

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Release 2023.1 (January 2023)