P4HB Human

Prolyl 4-Hydroxylase is a tetrameric enzyme composed of two alpha (α) and two beta (β) subunits. The beta subunit, also known as Protein Disulfide-Isomerase (PDI), plays a critical role in maintaining the enzyme in a soluble and active state . The alpha subunits contain the catalytic sites necessary for the hydroxylation reaction .

The enzyme’s primary function is to hydroxylate proline residues in the repeating sequence Xaa-Pro-Gly found in collagen. This hydroxylation is crucial for the proper folding and thermal stability of collagen . Without this modification, collagen would not be able to maintain its structural integrity, leading to various connective tissue disorders.

The recombinant production of human Prolyl 4-Hydroxylase Beta (P4HB) has been a significant advancement in biotechnology. Recombinant P4HB is produced using various expression systems, including Escherichia coli (E. coli) and transgenic plants . These systems allow for the large-scale production of the enzyme, which is essential for research and therapeutic applications.

In E. coli, the production of recombinant P4HB involves the co-expression of both the alpha and beta subunits. This co-expression ensures the formation of the active tetrameric enzyme. The use of specific promoters and optimized growth conditions, such as cell density and oxygen supply, are critical factors in maximizing the yield of soluble P4HB .

Recombinant P4HB has numerous applications in both research and industry. It is used in the production of hydroxylated collagen, which has enhanced thermal stability and is suitable for various medical and industrial applications . Hydroxylated collagen is used in tissue engineering, drug delivery systems, and as a biomaterial for wound healing.

Additionally, P4HB is being explored as a potential target in cancer therapy. The enzyme’s role in maintaining the stability of the extracellular matrix makes it a promising candidate for therapeutic interventions .