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Literature summary for 4.6.1.19 extracted from
- The 1.8 A crystal structure of ACTIBIND suggests a mode of action for T2 ribonucleases as antitumorigenic agents (2012), J. Med. Chem., 55, 1013-1020.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified enzyme, X-ray diffraction structure determination and analysis at 1.8 A resolution, modeling | Rattus norvegicus |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 27660 | - |
x * 30558, glyosylated enzyme, mass spectrometry, x * 27660, sequence calculation | Rattus norvegicus |
| 30558 | - |
x * 30558, glyosylated enzyme, mass spectrometry, x * 27660, sequence calculation | Rattus norvegicus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Homo sapiens | RNases are ubiquitous and efficient enzymes that hydrolyze RNA to 3' mononucleotides | ? | - |
? |  |
| additional information | Rattus norvegicus | RNases are ubiquitous and efficient enzymes that hydrolyze RNA to 3' mononucleotides | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
| Rattus norvegicus | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | the enzyme is a thermostable glycoprotein with two N-glycosylation sites at Asn74 and at Asn83. Both asparagine residues are part of an Asn-Xaa-Ser/Thr motif which is typical for N-glycosylation site | Rattus norvegicus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | RNases are ubiquitous and efficient enzymes that hydrolyze RNA to 3' mononucleotides | Homo sapiens | ? | - |
? | |
| additional information | RNases are ubiquitous and efficient enzymes that hydrolyze RNA to 3' mononucleotides | Rattus norvegicus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 30558, glyosylated enzyme, mass spectrometry, x * 27660, sequence calculation | Rattus norvegicus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ACTIBIND | - |
Rattus norvegicus |
| RNaseT2 | - |
Homo sapiens |
| T2 ribonuclease | - |
Homo sapiens |
| T2 ribonuclease | - |
Rattus norvegicus |
| T2 RNase | - |
Homo sapiens |
| T2 RNase | - |
Rattus norvegicus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | the enzyme catalytic site, which is responsible for RNA degradation is composed of residues His51, His110, His115, Glu111, Trp54, Asp56, and Tyr62 which are involved in binding the target base. These residues are located on the surface of the molecule, thereby creating a cavity for the substrate | Rattus norvegicus |
| physiological function | RNases are ubiquitous and efficient enzymes that hydrolyze RNA to 3' mononucleotides and also possess antitumorigenic and antiangiogenic activities. The enzyme binds actin and interferes with the cytoskeletal network structure, thereby inhibiting cell motility and invasiveness in cancer and in endothelial cells. Two structural elements create the binding site for actin, that is composed of one cysteine residue and one conserved amino acid region. The actin binding sites possibly interfere with the cytoskeleton network structure and as such may be responsible for the antitumorigenic and antiangiogenic activities of the enzyme | Homo sapiens |
| physiological function | RNases are ubiquitous and efficient enzymes that hydrolyze RNA to 3' mononucleotides and also possess antitumorigenic and antiangiogenic activities. The enzyme binds actin and interferes with the cytoskeletal network structure, thereby inhibiting cell motility and invasiveness in cancer and in endothelial cells. Two structural elements create the binding site for actin, that is composed of one cysteine residue and one conserved amino acid region. The actin binding sites possibly interfere with the cytoskeleton network structure and as such may be responsible for the antitumorigenic and antiangiogenic activities of the enzyme. The enzyme inhibits human umbilical vein endothelial cell tube formation | Rattus norvegicus |
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