Guanylyltransferase

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Guanylyl transferases are enzymes that transfer a guanosine mono phosphate group, usually from GTP to another molecule, releasing pyrophosphate. Many eukaryotic guanylyl transferases are capping enzymes that catalyze the formation of the 5' cap in the co-transcriptional modification of messenger RNA. Because the 5' end of the RNA molecule ends in a phosphate group, the bond formed between the RNA and the GTP molecule is an unusual 5'-5' triphosphate linkage, instead of the 3'-5' linkages between the other nucleotides that form an RNA strand. In capping enzymes, a highly conserved lysine residue serves as the catalytic residue that forms a covalent enzyme-GMP complex. [1]

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The transfer RNA (tRNA) for histidine is unique among eukaryotic tRNAs in requiring the addition of a guanine nucleotide before being aminoacylated by the histidine tRNA synthetase. The yeast guanylyl transferase specific to tRNAHis is unique in being the only known non-tRNA synthetase enzyme that specifically recognizes the tRNA anticodon. [2]

Guanylyl transferases also exist for transferring guanosine nucleotides to sugar molecules, such as mannose and fucose.[ citation needed ]

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<span class="mw-page-title-main">Guanosine triphosphate</span> Chemical compound

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<span class="mw-page-title-main">Ribonucleotide</span> Nucleotide containing ribose as its pentose component

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<span class="mw-page-title-main">Post-transcriptional modification</span> RNA processing within a biological cell

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<span class="mw-page-title-main">Capping enzyme</span>

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<span class="mw-page-title-main">GMP synthase</span>

Guanosine monophosphate synthetase, also known as GMPS is an enzyme that converts xanthosine monophosphate to guanosine monophosphate.

<span class="mw-page-title-main">Ribose-phosphate diphosphokinase</span> Class of enzymes

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In enzymology, a fucose-1-phosphate guanylyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a guanosine-triphosphate guanylyltransferase (EC 2.7.7.45) is an enzyme that catalyzes the chemical reaction

In enzymology, a mannose-1-phosphate guanylyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a mannose-1-phosphate guanylyltransferase (GDP) is an enzyme that catalyzes the chemical reaction

In enzymology, a mRNA guanylyltransferase is an enzyme that catalyzes the chemical reaction

Amino acid activation refers to the attachment of an amino acid to its respective transfer RNA (tRNA). The reaction occurs in the cell cytosol and consists of two steps: first, the enzyme aminoacyl tRNA synthetase catalyzes the binding of adenosine triphosphate (ATP) to a corresponding amino acid, forming a reactive aminoacyl adenylate intermediate and releasing inorganic pyrophosphate (PPi). Subsequently, aminoacyl tRNA synthetase binds the AMP-amino acid to a tRNA molecule, releasing AMP and attaching the amino acid to the tRNA. The resulting aminoacyl-tRNA is said to be charged.

tRNA(His) guanylyltransferase is an enzyme with systematic name p-tRNA(His):GTP guanylyltransferase (ATP-hydrolysing). This enzyme catalyses the following chemical reaction

References

  1. Fresco LD, Buratowski S. (1994). Active site of the mRNA-capping enzyme guanylyltransferase from Saccharomyces cerevisiae: similarity to the nucleotidyl attachment motif of DNA and RNA ligases. Proc Natl Acad Sci USA 91(14): 6624–6628.
  2. Jackman JE, Phizicky EM. (2006). tRNAHis guanylyltransferase adds G–1 to the 5' end of tRNAHis by recognition of the anticodon, one of several features unexpectedly shared with tRNA synthetases. RNA 12:1007-1014.