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Literature summary extracted from

  • Lampitella, E.; Landi, N.; Oliva, R.; Gaglione, R.; Bosso, A.; De Lise, F.; Ragucci, S.; Arciello, A.; Petraccone, L.; Pizzo, E.; Del Vecchio, P.; Di Maro, A.
    Toxicity and membrane perturbation properties of the ribotoxin-like protein Ageritin (2021), J. Biochem., 170, 473-482.
    View publication on PubMed

General Stability

EC Number General Stability Organism
4.6.1.23 ageritin presents high thermal and chemical stability Cyclocybe aegerita

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.6.1.23 additional information
-
 additional information thermodynamics of enzyme reaction with liposomes Cyclocybe aegerita

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.6.1.23 Mg2+ dependent on Cyclocybe aegerita
4.6.1.23 additional information ageritin shows strict metal ion-binding requirements for its ribonucleolytic activity, such as Zn2+ and Mg2+ Cyclocybe aegerita
4.6.1.23 Zn2+ dependent on Cyclocybe aegerita

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.23 Cyclocybe aegerita
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.6.1.23 native enzyme from fruiting bodies by precipitation at pH 4.0, cation exchange chromatography, gel filtration, and again cation exchange chromatography, to homogeneity Cyclocybe aegerita

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.6.1.23 basidiocarp
-
 Cyclocybe aegerita
-
4.6.1.23 fruit body
-
 Cyclocybe aegerita
-

Subunits

EC Number Subunits Comment Organism
4.6.1.23 additional information ageritin is a basic protein of 135 amino acid residues, with a single free cysteinyl residue in contrast to canonical ribotoxins that have two disulphide bridges Cyclocybe aegerita

Synonyms

EC Number Synonyms Comment Organism
4.6.1.23 ageritin
-
 Cyclocybe aegerita
4.6.1.23 ribotoxin-like protein
-
 Cyclocybe aegerita

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.6.1.23 additional information
-
 ageritin presents high thermal stability Cyclocybe aegerita

General Information

EC Number General Information Comment Organism
4.6.1.23 additional information ageritin is a basic protein of 135 amino acid residues, with a single free cysteinyl residue in contrast to canonical ribotoxins that have two disulphide bridges Cyclocybe aegerita
4.6.1.23 physiological function ageritin is a specific ribonuclease, isolated from the basidiomycete fungus Agrocybe aegerita, that cleaves ribosomal RNA resulting in an irreversibly block of protein synthesis. The extreme specificity of ageritin for rRNA is due to the cleavage of a single phosphodiester bond in a highly conserved region, known as sarcin-ricin loop (SRL), evolutionarily conserved from bacteria to mammalians, and involved in the binding of elongation factors. The SRL sequence is also the target of ribotoxins, specific extracellular ribonucleases, produced by several fungal ascomycetes species, such as Aspergillus giganteus, from which has been isolated alpha-sarcin, the prototype of this enzyme family. Ageritin and other ribotoxins are able to inhibit protein synthesis by releasing a small rRNA fragment known as alpha-fragment, when incubated with several eukaryotic and prokaryotic ribosomes. Analysis of the cytotoxicity of argeritin against simian-virus-40-transformed mouse fibroblasts (SVT2 cells) and the parental non-transformed BALB/c 3T3 cell lines. Ageritin shows selective cytotoxic activity. Internalization of ageritin in BALB/c 3T3 and SVT2 cells. Selective antitumor activity of ageritin. Interaction analysis of argeritin with model membranes shows that increasing ageritin concentrations lead to a progressive decrease of enthalpy change of the pre-transition peak, indicating a strong perturbation of the lipids head groups of the bilayer upon protein interaction Cyclocybe aegerita