Peptidase D is a single, non-glycosylated polypeptide chain composed of 516 amino acids, with a molecular mass of approximately 56.9 kDa . The recombinant form of this enzyme is typically produced in Escherichia coli (E. coli) and is often fused to a His-tag at the N-terminus to facilitate purification . The enzyme is stored in a sterile, colorless solution containing phosphate-buffered saline, glycerol, and dithiothreitol (DTT) to maintain its stability .
Peptidase D plays a pivotal role in collagen metabolism by recycling proline, an amino acid that constitutes over 20% of collagen . The enzyme catalyzes the hydrolysis of imidodipeptides, which are generated during the breakdown of collagen, into their constituent amino acids . This process is essential for collagen turnover, matrix remodeling, and protein metabolism .
The activity of Peptidase D is vital for several physiological processes, including:
Mutations in the PEPD gene can lead to prolidase deficiency, a rare autosomal recessive metabolic disorder characterized by defective wound healing and other symptoms . Additionally, alterations in Peptidase D activity have been observed in various pathological conditions, making it a valuable biochemical marker for disease severity .
For optimal stability, Peptidase D should be stored at -20°C for long-term use, with the addition of a carrier protein to prevent degradation . It is important to avoid multiple freeze-thaw cycles to maintain the enzyme’s activity .
In summary, Peptidase D (Human Recombinant) is a crucial enzyme in collagen metabolism, with significant roles in various physiological processes and clinical implications. Its recombinant form, produced in E. coli, provides a valuable tool for research and therapeutic applications.