BPHL is a Serine hydrolase that is a part of the AB hydrolase superfamily which catalyzes the hydrolytic activation of amino acid ester prodrugs of nucleoside analogs such as valacyclovir and valganciclovir. BPHL is expressed large quantities in liver and kidney and in minor quantities in heart, intestine and skeletal muscle. BPHL takes part in detoxification processes and is a specific alpha-amino acid ester hydrolase which favors small, hydrophobic, and aromatic side chains and does not have a strict necessity for the leaving group except for favoring a primary alcohol.
BPHL produced in E.Coli is a single, non-glycosylated polypeptide chain containing 275 amino acids (38-291a.a.) and having a molecular mass of 31.1kDa.
BPHL is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
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