| Record Information |
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| Version | 2.0 |
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| Creation Date | 2010-05-26 16:05:40 UTC |
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| Update Date | 2014-12-24 20:26:31 UTC |
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| Accession Number | T3D3773 |
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| Identification |
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| Common Name | alpha-Sarcin (Aspergillus giganteus) |
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| Class | Protein |
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| Description | alpha-Sarcin is a protein mycotoxin produced by the fungi Aspergillus giganteus and Aspergillus restrictus. It is a highly specific ribotoxin and inhibits protein synthesis by cleaving the 28S RNA and of eukaryotic ribosomes. (2, 3) |
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| Compound Type | - Amide
- Amine
- Fungal Toxin
- Mycotoxin
- Natural Compound
- Organic Compound
- Protein
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| Protein Structure |  |
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| Synonyms | | Synonym | | a-Sarcin | | alpha-Sarcin | | Ribonuclease alpha-sarcin | | rRNA endonuclease |
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| Chemical Formula | Not Available |
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| Average Molecular Mass | 19724.200 g/mol |
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| CAS Registry Number | 86243-64-3 |
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| Sequence | Not Available |
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| Chemical Taxonomy |
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| Description | Not Available |
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| Kingdom | Organic Compounds |
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| Super Class | Organic Acids |
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| Class | Carboxylic Acids and Derivatives |
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| Sub Class | Amino Acids, Peptides, and Analogues |
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| Direct Parent | Peptides |
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| Alternative Parents | Not Available |
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| Substituents | Not Available |
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| Molecular Framework | Not Available |
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| External Descriptors | Not Available |
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| Biological Properties |
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| Status | Detected and Not Quantified |
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| Origin | Exogenous |
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| Cellular Locations | Not Available |
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| Biofluid Locations | Not Available |
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| Tissue Locations | Not Available |
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| Pathways | Not Available |
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| Applications | Not Available |
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| Biological Roles | Not Available |
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| Chemical Roles | Not Available |
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| Physical Properties |
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| State | Liquid |
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| Appearance | Clear solution. |
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| Experimental Properties | | Property | Value |
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| Melting Point | Not Available | | Boiling Point | Not Available | | Solubility | >10 mg/mL | | LogP | Not Available |
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| Predicted Properties | Not Available |
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| Spectra |
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| Spectra | | Spectrum Type | Description | Splash Key | Deposition Date | View |
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| Toxicity Profile |
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| Route of Exposure | Oral, dermal, inhalation, and parenteral (contaminated drugs). (5) |
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| Mechanism of Toxicity | alpha-Sarcin is a highly specific ribotoxin that inhibits protein synthesis by cleaving a single phosphodiester bond in the sarcin/ricin loop (SRL) of the 23S−28S rRNA of eukaryotic ribosomes. The sequence around this cleavage site is a binding site for elongation factors, and is conserved in all cytoplasmic ribosomes. In order to cleave this site, alpha-sarcin binds to the rRNA by forming an electrostatic complex using specific residues on its active site face. This cleavage prevents the binding of elongation factors to the ribosome, halts protein synthesis, and eventually leads to apoptotic cell death. (1, 2, 3, 4) |
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| Metabolism | Free toxin may be removed by opsonization via the reticuloendothelial system (primarily the liver and kidneys) or it may be degraded through cellular internalization via the lysosomes. Lysosomes are membrane-enclosed organelles that contain an array of digestive enzymes, including several proteases. |
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| Toxicity Values | Not Available |
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| Lethal Dose | Not Available |
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| Carcinogenicity (IARC Classification) | No indication of carcinogenicity to humans (not listed by IARC). |
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| Uses/Sources | alpha-Sarcin is a protein mycotoxin produced by the fungi Aspergillus giganteus and Aspergillus restrictus. (2) |
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| Minimum Risk Level | Not Available |
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| Health Effects | alpha-Sarcin is a cytotoxic ribotoxin, causing cell death by inactivating eukaryotic ribosomes. (2) |
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| Symptoms | Not Available |
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| Treatment | Not Available |
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| Normal Concentrations |
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| Not Available |
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| Abnormal Concentrations |
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| Not Available |
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| External Links |
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| DrugBank ID | Not Available |
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| HMDB ID | Not Available |
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| PubChem Compound ID | Not Available |
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| ChEMBL ID | Not Available |
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| ChemSpider ID | Not Available |
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| KEGG ID | Not Available |
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| UniProt ID | P00655 |
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| OMIM ID | |
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| ChEBI ID | Not Available |
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| BioCyc ID | Not Available |
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| CTD ID | Not Available |
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| Stitch ID | Not Available |
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| PDB ID | 1DE3 |
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| ACToR ID | Not Available |
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| Wikipedia Link | Not Available |
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| References |
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| Synthesis Reference | Not Available |
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| MSDS | Not Available |
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| General References | - Korennykh AV, Plantinga MJ, Correll CC, Piccirilli JA: Linkage between substrate recognition and catalysis during cleavage of sarcin/ricin loop RNA by restrictocin. Biochemistry. 2007 Nov 6;46(44):12744-56. Epub 2007 Oct 12. [17929942 ]
- Martinez-Ruiz A, Kao R, Davies J, Martinez del Pozo A: Ribotoxins are a more widespread group of proteins within the filamentous fungi than previously believed. Toxicon. 1999 Nov;37(11):1549-63. [10482390 ]
- Sacco G, Drickamer K, Wool IG: The primary structure of the cytotoxin alpha-sarcin. J Biol Chem. 1983 May 10;258(9):5811-8. [6343394 ]
- Correll CC, Yang X, Gerczei T, Beneken J, Plantinga MJ: RNA recognition and base flipping by the toxin sarcin. J Synchrotron Radiat. 2004 Jan 1;11(Pt 1):93-6. Epub 2003 Nov 28. [14646144 ]
- Peraica M, Domijan AM: Contamination of food with mycotoxins and human health. Arh Hig Rada Toksikol. 2001 Mar;52(1):23-35. [11370295 ]
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| Gene Regulation |
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| Up-Regulated Genes | Not Available |
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| Down-Regulated Genes | Not Available |
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