Recombinant Mycoplasma mobile peptidyl-tRNA hydrolase (Pth) is an enzyme derived from the bacterium Mycoplasma mobile, which is known for its unique ability to move using a gliding mechanism. Peptidyl-tRNA hydrolases are enzymes that play a crucial role in the recycling of transfer RNA (tRNA) by cleaving the peptide bond between the amino acid and tRNA, thereby releasing the tRNA for further rounds of protein synthesis. This process is essential for maintaining cellular homeostasis and ensuring efficient protein synthesis.
Peptidyl-tRNA hydrolase is vital in bacteria, including Mycoplasma mobile, as it rescues stalled ribosomes by releasing unfinished peptides from tRNA. This function is critical for maintaining a pool of free tRNA molecules necessary for ongoing protein synthesis. Without Pth, peptidyl-tRNA accumulates, leading to tRNA starvation and impaired cellular growth .
The mechanism of action of peptidyl-tRNA hydrolase involves the hydrolysis of the ester bond between the peptide chain and tRNA. This process is facilitated by specific structural components of the enzyme, including conserved residues within its catalytic site. The enzyme's dynamic nature allows it to undergo conformational changes to accommodate substrates, ensuring precise hydrolysis .
While specific data on recombinant Mycoplasma mobile Pth is limited, research on bacterial Pth in general highlights its significance in bacterial physiology and its potential as a drug target. Studies have shown that reducing Pth levels in bacteria like Mycobacterium tuberculosis increases sensitivity to certain antibiotics, underscoring the enzyme's role in maintaining translation fidelity and cellular stress response pathways .
This enzyme's natural substrate is likely peptidyl-tRNAs released from the ribosome during protein synthesis.
KEGG: mmo:MMOB5410
STRING: 267748.MMOB5410