TRNA sulfurtransferase

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tRNA sulfurtransferase
Identifiers
EC no. 2.8.1.4
CAS no. 9055-57-6
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BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
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Gene Ontology AmiGO / QuickGO
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NCBI proteins

In enzymology, a tRNA sulfurtransferase (EC 2.8.1.4) is an enzyme that catalyzes the chemical reaction

L-cysteine + 'activated' tRNA L-serine + tRNA containing a thionucleotide

Thus, the two substrates of this enzyme are L-cysteine and 'activated' tRNA, whereas its two products are L-serine and tRNA containing a thionucleotide.

This enzyme belongs to the family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is L-cysteine:tRNA sulfurtransferase. Other names in common use include transfer ribonucleate sulfurtransferase, RNA sulfurtransferase, ribonucleate sulfurtransferase, transfer RNA sulfurtransferase, and transfer RNA thiolase.

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.

<span class="mw-page-title-main">Catalytic triad</span> Set of three coordinated amino acids

A catalytic triad is a set of three coordinated amino acids that can be found in the active site of some enzymes. Catalytic triads are most commonly found in hydrolase and transferase enzymes. An acid-base-nucleophile triad is a common motif for generating a nucleophilic residue for covalent catalysis. The residues form a charge-relay network to polarise and activate the nucleophile, which attacks the substrate, forming a covalent intermediate which is then hydrolysed to release the product and regenerate free enzyme. The nucleophile is most commonly a serine or cysteine amino acid, but occasionally threonine or even selenocysteine. The 3D structure of the enzyme brings together the triad residues in a precise orientation, even though they may be far apart in the sequence.

Cysteine metabolism refers to the biological pathways that consume or create cysteine. The pathways of different amino acids and other metabolites interweave and overlap to creating complex systems.

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References