Aminoacyl-tRNA hydrolase

Last updated
aminoacyl-tRNA hydrolase
Identifiers
EC no. 3.1.1.29
CAS no. 9054-98-2
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

The enzyme aminoacyl-tRNA hydrolase (EC 3.1.1.29) catalyzes the reaction

N-substituted aminoacyl-tRNA + H2O N-substituted amino acid + tRNA

This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is aminoacyl-tRNA aminoacylhydrolase. Other names in common use include aminoacyl-transfer ribonucleate hydrolase, N-substituted aminoacyl transfer RNA hydrolase, and peptidyl-tRNA hydrolase.

Structural studies

As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1RYB, 1WN2, 1XTY, 2D3K, 2E1B, 2PTH, 2Z2I, 2Z2J, and 2Z2K.

Related Research Articles

<span class="mw-page-title-main">Aminoacyl tRNA synthetase</span> Class of enzymes

An aminoacyl-tRNA synthetase, also called tRNA-ligase, is an enzyme that attaches the appropriate amino acid onto its corresponding tRNA. It does so by catalyzing the transesterification of a specific cognate amino acid or its precursor to one of all its compatible cognate tRNAs to form an aminoacyl-tRNA. In humans, the 20 different types of aa-tRNA are made by the 20 different aminoacyl-tRNA synthetases, one for each amino acid of the genetic code.

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

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 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 histidine-tRNA ligase is an enzyme that catalyzes the chemical reaction

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

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

In enzymology, a valine—tRNA ligase 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.

References