Valine--tRNA ligase, also known as Valyl-tRNA synthetase, is an enzyme responsible for attaching the amino acid valine to its corresponding transfer RNA (tRNA) molecule. This process is crucial for protein synthesis, as it ensures that the genetic code is accurately translated into the correct amino acid sequence in proteins.
Nitrosomonas europaea is a gram-negative bacterium that plays a significant role in the biogeochemical nitrogen cycle by oxidizing ammonia to nitrite. It is an obligate chemolithoautotroph, meaning it derives its energy from the oxidation of inorganic compounds and uses carbon dioxide as its carbon source .
Recombinant proteins are produced through genetic engineering techniques where the gene encoding a specific protein is inserted into a host organism, such as bacteria or yeast, which then expresses the protein. Recombinant Valine--tRNA ligase from Clostridium perfringens is available, but there is no specific information on a recombinant version from Nitrosomonas europaea in the provided search results .
Given the lack of specific information on "Recombinant Nitrosomonas europaea Valine--tRNA ligase (valS), partial," potential research directions could include:
Expression and Purification: Investigating the expression and purification of Valine--tRNA ligase in Nitrosomonas europaea using recombinant DNA technology.
Enzymatic Activity: Studying the enzymatic activity and specificity of the recombinant enzyme to understand its role in protein synthesis within Nitrosomonas europaea.
Structural Analysis: Conducting structural studies to compare the enzyme's structure with other Valine--tRNA ligases and understand its unique features.
Since specific data on "Recombinant Nitrosomonas europaea Valine--tRNA ligase (valS), partial" is not available, here is a general table format that could be used for such a compound if data were available:
Characteristics | Description |
---|---|
Source Organism | Nitrosomonas europaea |
Expression Host | (e.g., E. coli, Yeast) |
Purity | (e.g., >85% by SDS-PAGE) |
Sequence | Specific amino acid sequence |
Storage Conditions | (e.g., -20°C/-80°C) |
Function: Catalyzes the attachment of valine to tRNA(Val). To prevent errors from the incorporation of similar amino acids like threonine, ValRS possesses post-transfer editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
KEGG: neu:NE0444
STRING: 228410.NE0444