Phenylalanyl-TRNA Synthetase Beta (FARSB) is a crucial enzyme in the process of protein synthesis. It belongs to the aminoacyl-tRNA synthetase class IIc subfamily and plays a significant role in attaching the amino acid phenylalanine to its corresponding tRNA molecule. This enzyme is highly conserved across different species, indicating its essential function in cellular biology .
The FARSB enzyme is a heterotetramer, consisting of two catalytic alpha subunits and two regulatory beta subunits. The beta subunits are responsible for the regulatory functions of the enzyme, while the alpha subunits carry out the catalytic activity. In the presence of ATP, the enzyme attaches L-phenylalanine to the terminal adenosine of the appropriate tRNA, a critical step in the translation process .
Human recombinant FARSB can be expressed in various systems, including Escherichia coli. The cDNAs of the alpha and beta subunits are cloned into expression vectors, such as pET-21b(+) and pET-28b(+), to produce the enzyme in a recombinant form. This allows for the study and utilization of the enzyme in various biochemical and medical research applications .
FARSB is involved in the tRNA aminoacylation pathway, which is essential for protein translation. Proper functioning of this enzyme ensures the accurate incorporation of phenylalanine into growing polypeptide chains, which is vital for the synthesis of functional proteins. Mutations or dysregulation of the FARSB gene can lead to various diseases, including Rajab Interstitial Lung Disease with Brain Calcifications and liver cirrhosis .