BPHL Protein, Human (P.pastoris, His-Myc)

The BPHL protein is a serine hydrolase that catalyzes the hydrolytic activation of amino acid ester prodrugs, such as nucleoside analogs such as valacyclovir and valganciclovir. It converts valacyclovir to acyclovir via hydrolysis. BPHL Protein, Human (P.pastoris, His-Myc) is the recombinant human-derived BPHL protein, expressed by P. pastoris , with N-His, C-Myc labeled tag. The total length of BPHL Protein, Human (P.pastoris, His-Myc) is 254 a.a., with molecular weight of ~32.3 kDa.

BPHL protein, a serine hydrolase, serves as a catalyst for the hydrolytic activation of amino acid ester prodrugs, exemplified by nucleoside analogs like valacyclovir and valganciclovir. Notably, it facilitates the conversion of valacyclovir to acyclovir through hydrolysis. Beyond its role in drug activation, BPHL is implicated in potential detoxification processes. As a specific alpha-amino acid ester hydrolase, it displays a preference for small, hydrophobic, and aromatic side chains, without imposing strict requirements on the leaving group, except for a preference toward a primary alcohol. Existing as a monomer, BPHL may also engage in the formation of homodimers.

Human

P. pastoris

N-His;C-Myc

Q86WA6 (38S-291Q)

670  [NCBI]

SVTSAKVAVNGVQLHYQQTGEGDHAVLLLPGMLGSGETDFGPQLKNLNKKLFTVVAWDPRGYGHSRPPDRDFPADFFERDAKDAVDLMKALKFKKVSLLGWSDGGITALIAAAKYPSYIHKMVIWGANAYVTDEDSMIYEGIRDVSKWSERTRKPLEALYGYDYFARTCEKWVDGIRQFKHLPDGNICRHLLPRVQCPALIVHGEKDPLVPRFHADFIHKHVKGSRLHLMPEGKHNLHLRFADEFNKLAEDFLQ

Approximately 32.3 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.