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Literature summary for 4.6.1.23 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
Search for more literature for 4.6.1.23

General Stability

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

KM Value [mM]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Cyclocybe aegerita
-
-
-

Purification (Commentary)

Purification (Comment) Organism
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

Source Tissue Comment Organism Textmining
basidiocarp
-
 Cyclocybe aegerita
-
fruit body
-
 Cyclocybe aegerita
-

Subunits

Subunits Comment Organism
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

Synonyms Comment Organism
ageritin
-
 Cyclocybe aegerita
ribotoxin-like protein
-
 Cyclocybe aegerita

Temperature Stability [°C]

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

General Information

General Information Comment Organism
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
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