| IED ID | IndEnz0005001208 |
| Enzyme Type ID | lipase001208 |
| Protein Name |
Valacyclovir hydrolase VACVase Valacyclovirase EC 3.1.-.- Biphenyl hydrolase-like protein Biphenyl hydrolase-related protein Bph-rp Breast epithelial mucin-associated antigen MCNAA |
| Gene Name | BPHL MCNAA |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MVAVLGGRGVLRLRLLLSALKPGIHVPRAGPAAAFGTSVTSAKVAVNGVQLHYQQTGEGDHAVLLLPGMLGSGETDFGPQLKNLNKKLFTVVAWDPRGYGHSRPPDRDFPADFFERDAKDAVDLMKALKFKKVSLLGWSDGGITALIAAAKYPSYIHKMVIWGANAYVTDEDSMIYEGIRDVSKWSERTRKPLEALYGYDYFARTCEKWVDGIRQFKHLPDGNICRHLLPRVQCPALIVHGEKDPLVPRFHADFIHKHVKGSRLHLMPEGKHNLHLRFADEFNKLAEDFLQ |
| Enzyme Length | 291 |
| Uniprot Accession Number | Q86WA6 |
| Absorption | |
| Active Site | ACT_SITE 139; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:18256025"; ACT_SITE 244; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10037, ECO:0000269|PubMed:18256025"; ACT_SITE 272; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10037, ECO:0000269|PubMed:18256025" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.1.-.- |
| Enzyme Function | FUNCTION: Serine hydrolase that catalyzes the hydrolytic activation of amino acid ester prodrugs of nucleoside analogs such as valacyclovir and valganciclovir. Activates valacyclovir to acyclovir. May play a role in detoxification processes. It is a specific alpha-amino acid ester hydrolase that prefers small, hydrophobic, and aromatic side chains and does not have a stringent requirement for the leaving group other than preferring a primary alcohol. {ECO:0000269|PubMed:18256025}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (1); Beta strand (10); Chain (1); Domain (1); Helix (14); Modified residue (13); Mutagenesis (3); Sequence conflict (2); Signal peptide (1); Site (1); Turn (2) |
| Keywords | 3D-structure;Acetylation;Alternative splicing;Direct protein sequencing;Hydrolase;Reference proteome;Signal |
| Interact With | P62508-3 |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 86; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q8R164; MOD_RES 119; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q8R164; MOD_RES 126; /note=N6-acetyllysine; alternate; /evidence=ECO:0007744|PubMed:19608861; MOD_RES 126; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q8R164; MOD_RES 184; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q8R164; MOD_RES 191; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q8R164; MOD_RES 191; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q8R164; MOD_RES 217; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q8R164; MOD_RES 243; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q8R164; MOD_RES 260; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q8R164; MOD_RES 260; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q8R164; MOD_RES 271; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q8R164; MOD_RES 271; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q8R164 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..37; /evidence=ECO:0000269|PubMed:12732646 |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 2OCG; 2OCI; 2OCK; 2OCL; |
| Mapped Pubmed ID | 20237496; 20877624; 25333274; |
| Motif | |
| Gene Encoded By | |
| Mass | 32,543 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |