Enzymes
| UniProtKB help_outline | 46 proteins |
| Enzyme class help_outline |
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Reaction participants Show >> << Hide
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Namehelp_outline
a ribonucleotidyl-ribonucleotide-RNA
Identifier
RHEA-COMP:17355
Reactive part
help_outline
- Name help_outline ribonucleotide-ribonucleotide residue Identifier CHEBI:173118 Charge -2 Formula C10H14O12P2R2 SMILEShelp_outline *[C@@H]1O[C@H](COP(*)(=O)[O-])[C@H]([C@H]1O)OP(OC[C@H]2O[C@@H](*)[C@@H]([C@@H]2O*)O)([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
a 3'-end 3'-phospho-ribonucleotide-RNA
Identifier
RHEA-COMP:10463
Reactive part
help_outline
- Name help_outline a 3'-terminal ribonucleotide 3'-phosphate residue Identifier CHEBI:83062 Charge -3 Formula C5H7O9P2R SMILEShelp_outline O[C@H]1[C@H]([*])O[C@H](COP([O-])(-*)=O)[C@H]1OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
a 5'-end dephospho-ribonucleoside-RNA
Identifier
RHEA-COMP:13936
Reactive part
help_outline
- Name help_outline 5'-end 5'-dephospho ribonucleotide residue Identifier CHEBI:138284 Charge 0 Formula C5H8O4R SMILEShelp_outline [C@@H]1([C@H]([C@@H](O[C@@H]1CO)*)O)O* 2D coordinates Mol file for the small molecule Search links Involved in 9 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:68052 | RHEA:68053 | RHEA:68054 | RHEA:68055 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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STUDIES ON THE FORMATION OF TOBACCO MOSAIC VIRUS RIBONUCLEIC ACID. VI. MODE OF DEGRADATION OF HOST RIBONUCLEIC ACID TO RIBONUCLEOSIDES AND THEIR CONVERSION TO RIBONUCLEOSIDE 5'-PHOSPHATES.
REDDI K.K., MAUSER L.J.
Proc Natl Acad Sci U S A 53:607-613(1965) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Purification, molecular and enzymic characterization of an acid RNase from the insect Ceratitis capitata.
Garcia-Segura J.M., Orozco M.M., Fominaya J.M., Gavilanes J.G.
An acid ribonuclease has been purified from the insect Ceratitis capitata. The specific activity of the purified enzyme is 580 units/mg. This enzyme is a single polypeptide chain of about 35.5 kDa, containing only one disulfide bridge and no free -SH groups. The A0.1%1cm at 280 nm is 1.90. The hyd ... >> More
An acid ribonuclease has been purified from the insect Ceratitis capitata. The specific activity of the purified enzyme is 580 units/mg. This enzyme is a single polypeptide chain of about 35.5 kDa, containing only one disulfide bridge and no free -SH groups. The A0.1%1cm at 280 nm is 1.90. The hydrodynamic radius of the native enzyme is 2.5 nm. The secondary structure of this RNase is composed of 10% alpha-helix, 31% beta-structure and 59% aperiodic conformation with an average number of residues per helical segment of 10, based on circular dichroic measurements. Optimum parameters for the enzyme activity are pH 5.5, 0.15 M ionic strength and 40 degrees C. Divalent cations are not required for the enzymic catalysis. This enzyme has been characterized as cyclizing endoribonuclease. << Less
Eur J Biochem 158:367-372(1986) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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T2 Family ribonucleases: ancient enzymes with diverse roles.
Luhtala N., Parker R.
Ribonucleases of the T2 family are found in the genomes of protozoans, plants, bacteria, animals and viruses. A broad range of biological roles for these ribonucleases have been suggested, including scavenging of nucleic acids, degradation of self-RNA, serving as extra- or intracellular cytotoxins ... >> More
Ribonucleases of the T2 family are found in the genomes of protozoans, plants, bacteria, animals and viruses. A broad range of biological roles for these ribonucleases have been suggested, including scavenging of nucleic acids, degradation of self-RNA, serving as extra- or intracellular cytotoxins, and modulating host immune responses. Recently, RNaseT2 family members have been implicated in human pathologies such as cancer and parasitic diseases. Interestingly, certain functions of RNaseT2 family members are independent of their nuclease activity, suggesting that these proteins have additional functions. Moreover, humans lacking RNASET2 manifest a defect in neurological development, perhaps due to aberrant control of the immune system. We review the basic structure and function of RNaseT2 family members and their biological roles. << Less
Trends Biochem Sci 35:253-259(2010) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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The specificity of ribonuclease T2.
Uchida T., Egami F.
J Biochem 61:44-53(1967) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
Comments
Multi-step reaction: RHEA:67796 and RHEA:68056