BPHL Human
Biphenyl Hydrolase-Like (serine hydrolase), Bph-rp, Breast Epithelial Mucin-Associated Antigen, MCNAA, VACVASE, MGC41865, MGC125930.
Description
BPHL is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Biphenyl Hydrolase-Like (serine hydrolase), Bph-rp, Breast Epithelial Mucin-Associated Antigen, MCNAA, VACVASE, MGC41865, MGC125930.
Product Science Overview
Biphenyl Hydrolase-Like (BPHL) is a serine hydrolase enzyme that plays a significant role in the hydrolytic activation of amino acid ester prodrugs of nucleoside analogs, such as valacyclovir and valganciclovir. This enzyme is also known for its role in detoxification processes and has been identified as a highly efficient homocysteine thiolactonase (HCTLase).
The BPHL gene is located on chromosome 6 and encodes a protein that belongs to the serine protease family of hydrolytic enzymes. These enzymes are characterized by the presence of a serine residue in their active site, which is crucial for their catalytic activity. The BPHL protein has several aliases, including Valacyclovir Hydrolase, Biphenyl Hydrolase-Related Protein, and Valacyclovirase .
BPHL catalyzes the hydrolytic activation of amino acid ester prodrugs by cleaving the ester bond, thereby converting the prodrug into its active form. For instance, BPHL activates valacyclovir to acyclovir, an antiviral drug used to treat herpes infections. The enzyme prefers substrates with small, hydrophobic, and aromatic side chains and does not have a stringent requirement for the leaving group, other than preferring a primary alcohol .
In addition to its role in drug activation, BPHL has been identified as a highly efficient homocysteine thiolactonase. Homocysteine thiolactone (HCTL) is a reactive metabolite of homocysteine that can cause protein aggregation and malfunction, leading to cardiovascular, autoimmune, and neurological diseases. BPHL hydrolyzes HCTL, thereby detoxifying it and preventing its harmful effects .
Recombinant BPHL (rBPHL) is produced by expressing the BPHL gene in a host organism, such as Escherichia coli. The recombinant protein is then purified and characterized to study its structure and function. The catalytic efficiency of rBPHL for HCTL hydrolysis is significantly higher than that of other known HCTL detoxifying enzymes, such as paraoxonase-1 (PON1) and bleomycin hydrolase (Blmh) .
The ability of BPHL to activate antiviral prodrugs and detoxify harmful metabolites makes it a valuable target for clinical and pharmaceutical research. Understanding the structure and function of BPHL can lead to the development of more effective prodrugs and therapeutic strategies for diseases associated with homocysteine metabolism.
