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Biphenyl hydrolase-like

valacyclovirase, BPHL, Bph-rp, Biphenyl hydrolase-like
This gene encodes a member of the serine protease family of hydrolytic enzymes which contain a serine in their active site. The encoded protein may play a role in activation of the antiviral prodrug valacyclovir. Alternatively spliced transcript variants have been described.[provided by RefSeq, Jan 2009] (from NCBI)
Top mentioned proteins: ACID, CAN, HAD, PEPT1, Gli3
Papers on valacyclovirase
Synthesis and characterization of valyloxy methoxy luciferin for the detection of valacyclovirase and peptide transporter.
Lee et al., Ann Arbor, United States. In Bioorg Med Chem Lett, 2014
An amino acid ester derivative of luciferin (valoluc) was synthesized to mimic the transport and activation of valacyclovir.
Human valacyclovir hydrolase/biphenyl hydrolase-like protein is a highly efficient homocysteine thiolactonase.
Furlong et al., Seattle, United States. In Plos One, 2013
A homocysteine thiolactonase (HCTLase) was purified from human liver and identified by mass spectrometry (MS) as the previously described human biphenyl hydrolase-like protein (BPHL).
Increasing oral absorption of polar neuraminidase inhibitors: a prodrug transporter approach applied to oseltamivir analogue.
Amidon et al., Ann Arbor, United States. In Mol Pharm, 2013
Additionally, l-valyl prodrug was found to be a substrate for valacyclovirase (K(m) = 2.37 mM), suggesting a potential cell activation mechanism.
[Identification of interaction between BPHL and PML-C].
Wu et al., Chongqing, China. In Sichuan Da Xue Xue Bao Yi Xue Ban, 2013
OBJECTIVE: To explore the interaction between BPHL and PML-C by co-immunoprecipitation and yeast two-hybird system.
Targeted prodrugs in oral drug delivery: the modern molecular biopharmaceutical approach.
Karaman et al., Beersheba, Israel. In Expert Opin Drug Deliv, 2012
Targeting the oligopeptide transporter PEPT1 for absorption and the serine hydrolase valacyclovirase for activation will be presented as examples for the successful utilization of this approach.
Specificity of a prodrug-activating enzyme hVACVase: the leaving group effect.
Amidon et al., Ann Arbor, United States. In Mol Pharm, 2011
Human valacyclovirase (hVACVase) is a prodrug-activating enzyme for amino acid prodrugs including the antiviral drugs valacyclovir and valganciclovir.
Genomic analysis of expressed sequence tags in American black bear Ursus americanus.
Yan et al., Shanghai, China. In Bmc Genomics, 2009
Two genes, biphenyl hydrolase-like (BPHL) and CSRP3, contain positively selected sites in bear.
Chemical and enzymatic stability of amino acid prodrugs containing methoxy, ethoxy and propylene glycol linkers.
Amidon et al., Ann Arbor, United States. In Mol Pharm, 2009
Enzymatic hydrolysis of propylene glycol containing compounds was studied using Caco-2 homogenate as well as purified enzyme valacyclovirase.
Molecular basis of prodrug activation by human valacyclovirase, an alpha-amino acid ester hydrolase.
Amidon et al., Ann Arbor, United States. In J Biol Chem, 2008
Our structural insights show that human valacyclovirase has a unique binding mode and specificity for amino acid esters.
HNF4 alpha orchestrates a set of 14 genes to down-regulate cell proliferation in kidney cells.
Ryffel et al., Essen, Germany. In Biol Chem, 2008
In addition, the genes SEPP1, THEM2, BPHL, DSC2, ANK3, ALDH6A1, EPHX2, NELL2, EFHD1 and PROS1 are also part of the network of HNF4 alpha target genes that regulate proliferation in HEK293 cells.
Nucleoside ester prodrug substrate specificity of liver carboxylesterase.
Amidon et al., Ann Arbor, United States. In J Pharmacol Exp Ther, 2006
The newly characterized esterase valacyclovirase was several hundred-fold more efficient (up to 19,000-fold) than carboxylesterase in hydrolyzing amino acid esters but similar in apparent binding affinity.
Transcriptional analysis of the molecular basis of human kidney aging using cDNA microarray profiling.
Sarwal et al., Edmonton, Canada. In Kidney Int, 2005
The expression of six functionally significant genes was further validated by quantitative reverse transcription-polymerase chain reaction (RT-PCR) (FN1, MMP7, TNC, SERPIN3A, BPHL, CSPG2) in the experiment group and, subsequently, confirmed independently in 17 additional old and adult age-stratified test kidney samples.
Structure and specificity of a human valacyclovir activating enzyme: a homology model of BPHL.
Amidon et al., Ann Arbor, United States. In Mol Pharm, 2004
Biphenyl hydrolase-like (BPHL) protein is a novel serine hydrolase which has been identified as human valacyclovirase (VACVase), catalyzing the hydrolytic activation of valine ester prodrugs of the antiviral drugs acyclovir and ganciclovir as well as other amino acid ester prodrugs of therapeutic nucleoside analogues.
A novel nucleoside prodrug-activating enzyme: substrate specificity of biphenyl hydrolase-like protein.
Amidon et al., Ann Arbor, United States. In Mol Pharm, 2004
BPHL catalyzes the hydrolytic activation of the antiviral prodrugs valacyclovir and valganciclovir.
Identification of a human valacyclovirase: biphenyl hydrolase-like protein as valacyclovir hydrolase.
Amidon et al., Ann Arbor, United States. In J Biol Chem, 2003
BPHL is a serine hydrolase that catalyzes the hydrolytic activation of amino acid ester prodrugs of nuceloside analogs such as valacyclovir and valganciclovir.
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