Related Research Articles
Ribonuclease is a type of nuclease that catalyzes the degradation of RNA into smaller components. Ribonucleases can be divided into endoribonucleases and exoribonucleases, and comprise several sub-classes within the EC 2.7 and 3.1 classes of enzymes.
Ribonuclease H is a family of non-sequence-specific endonuclease enzymes that catalyze the cleavage of RNA in an RNA/DNA substrate via a hydrolytic mechanism. Members of the RNase H family can be found in nearly all organisms, from bacteria to archaea to eukaryotes.
In biochemistry, a ribonucleotide is a nucleotide containing ribose as its pentose component. It is considered a molecular precursor of nucleic acids. Nucleotides are the basic building blocks of DNA and RNA. The monomer itself from ribonucleotides forms the basic building blocks for RNA. However, the reduction of ribonucleotide, by enzyme ribonucleotide reductase (RNR), forms deoxyribonucleotide, which is the essential building block for DNA. There are several differences between DNA deoxyribonucleotides and RNA ribonucleotides. Successive nucleotides are linked together via phosphodiester bonds by 3'-5'.
Ribonuclease III (BRENDA 3.1.26.3) is a type of ribonuclease that recognizes dsRNA and cleaves it at specific targeted locations to transform them into mature RNAs. These enzymes are a group of endoribonucleases that are characterized by their ribonuclease domain, which is labelled the RNase III domain. They are ubiquitous compounds in the cell and play a major role in pathways such as RNA precursor synthesis, RNA Silencing, and the pnp autoregulatory mechanism.
Pancreatic ribonucleases are pyrimidine-specific endonucleases found in high quantity in the pancreas of certain mammals and of some reptiles.
Exoribonuclease II is an enzyme. This enzyme catalyses the following chemical reaction
The degradosome is a multiprotein complex present in most bacteria that is involved in the processing of ribosomal RNA and the degradation of messenger RNA and is regulated by Non-coding RNA. It contains the proteins RNA helicase B, RNase E and Polynucleotide phosphorylase.
In enzymology, a tRNA (guanine-N7-)-methyltransferase (EC 2.1.1.33) is an enzyme that catalyzes the chemical reaction
In enzymology, a tRNA sulfurtransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a glutamate-tRNA ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a glutamine-tRNA ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a methionine-tRNA ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a proline—tRNA ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a serine-tRNA ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a threonine-tRNA ligase is an enzyme that catalyzes the chemical reaction
TRNA dimethylallyltransferase is an enzyme with systematic name dimethylallyl-diphosphate: tRNA dimethylallyltransferase. This enzyme catalyses the following chemical reaction
Ribonuclease E is a bacterial ribonuclease that participates in the processing of ribosomal RNA and the chemical degradation of bulk cellular RNA.
Ribonuclease U2 is an enzyme. This enzyme catalyses the following chemical reaction
Ribonuclease V1 is a ribonuclease enzyme found in the venom of the Caspian cobra. It cleaves double-stranded RNA in a non-sequence-specific manner, usually requiring a substrate of at least six stacked nucleotides. Like many ribonucleases, the enzyme requires the presence of magnesium ions for activity.
Ribonuclease T is a ribonuclease enzyme involved in the maturation of transfer RNA and ribosomal RNA in bacteria, as well as in DNA repair pathways. It is a member of the DnaQ family of exonucleases and non-processively acts on the 3' end of single-stranded nucleic acids. RNase T is capable of cleaving both DNA and RNA, with extreme sequence specificity discriminating against cytosine at the 3' end of the substrate.
References
- ↑ García-Segura JM, Orozco MM, Fominaya JM, Gavilanes JG (July 1986). "Purification, molecular and enzymic characterization of an acid RNase from the insect Ceratitis capitata". European Journal of Biochemistry. 158 (2): 367–72. doi:10.1111/j.1432-1033.1986.tb09760.x. PMID 3732273.
- ↑ Heppel LA, Davies DR (1966). "Pig liver nuclei ribonuclease". In Cantoni GL (ed.). Procedures in Nucleic Acid Research. New York: Procedures in Nucleic Acid Research. pp. 31–36.
- ↑ Reddi KK, Mauser LJ (March 1965). "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". Proceedings of the National Academy of Sciences of the United States of America. 53 (3): 607–13. doi: 10.1073/pnas.53.3.607 . PMC 336984 . PMID 14338240.
- ↑ Uchida T, Egami F (January 1967). "The specificity of ribonuclease T2". Journal of Biochemistry. 61 (1): 44–53. doi:10.1093/oxfordjournals.jbchem.a128519. PMID 6048969.
