O-phospho-L-serine—tRNA ligase

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O-Phospho-L-serine—tRNA ligase
Identifiers
EC no. 6.1.1.27
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O-phospho-L-serine—tRNA ligase (EC 6.1.1.27, O-phosphoseryl-tRNA ligase, non-canonical O-phosphoseryl-tRNA synthetase, SepRS) is an enzyme with systematic name O-phospho-L-serine:tRNACys ligase (AMP-forming). [1] [2] This enzyme catalyses the following chemical reaction:

ATP + O-phospho-L-serine + tRNACys AMP + diphosphate + O-phospho-L-seryl-tRNACys

In organisms like Archaeoglobus fulgidus , this enzyme ligates O-phosphoserine to tRNACys.

Related Research Articles

In molecular biology, biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined to form macromolecules. This process often consists of metabolic pathways. Some of these biosynthetic pathways are located within a single cellular organelle, while others involve enzymes that are located within multiple cellular organelles. Examples of these biosynthetic pathways include the production of lipid membrane components and nucleotides. Biosynthesis is usually synonymous with anabolism.

In enzymology, an alanine—tRNA ligase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Arginine—tRNA ligase</span>

In enzymology, an arginine—tRNA ligase is an enzyme that catalyzes the chemical reaction

In enzymology, an asparagine-tRNA ligase is an enzyme that catalyzes the chemical reaction

Aspartate—tRNAAsn ligase is an enzyme with systematic name L-aspartate:tRNAAsx ligase (AMP-forming). This enzyme catalyses the following chemical reaction

In enzymology, an aspartate—tRNA ligase is an enzyme that catalyzes the chemical reaction

In enzymology, a cysteine—tRNA ligase is an enzyme that catalyzes the chemical reaction

In enzymology, a histidine-tRNA ligase is an enzyme that catalyzes the chemical reaction

In enzymology, a lysine—tRNA ligase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Methionine—tRNA ligase</span>

In enzymology, a methionine—tRNA ligase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Phenylalanine—tRNA ligase</span>

In enzymology, a phenylalanine—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

In enzymology, a tryptophan-tRNA ligase is an enzyme that catalyzes the chemical reaction

O-phospho-L-seryl-tRNA:Cys-tRNA synthase is an enzyme with systematic name O-phospho-L-seryl-tRNACys:hydrogen sulfide 2-aminopropanoate transferase. This enzyme catalyses the following chemical reaction

O-phosphoseryl-tRNASec kinase is an enzyme with systematic name ATP:L-seryl-tRNASec O-phosphotransferase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">O-phospho-L-seryl-tRNASec:L-selenocysteinyl-tRNA synthase</span>

O-phospho-L-seryl-tRNASec:L-selenocysteinyl-tRNA synthase is an enzyme with systematic name selenophosphate:O-phospho-L-seryl-tRNASec selenium transferase. This enzyme catalyses the following chemical reaction

TRNAIle-lysidine synthase (EC 6.3.4.19, TilS, mesJ (gene), yacA (gene), isoleucine-specific transfer ribonucleate lysidine synthetase, tRNAIle-lysidine synthetase) is an enzyme with systematic name L-lysine:(tRNAIle2)-cytidine34 ligase (AMP-forming). This enzyme catalyses the following chemical reaction

References

  1. ↑ Fukunaga R, Yokoyama S (April 2007). "Structural insights into the first step of RNA-dependent cysteine biosynthesis in archaea". Nature Structural & Molecular Biology. 14 (4): 272–9. doi:10.1038/nsmb1219. PMID   17351629. S2CID   10959763.
  2. ↑ Hauenstein SI, Perona JJ (August 2008). "Redundant synthesis of cysteinyl-tRNACys in Methanosarcina mazei". The Journal of Biological Chemistry. 283 (32): 22007–17. doi: 10.1074/jbc.M801839200 . PMC   2494925 . PMID   18559341.
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