Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.52 (PNGase F)
 1,527 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have identified three Marek's disease virus (MDV) open reading frames (ORFs) within the BamHI D fragment of MDV genome. The predicted polypeptides are homologous to UL1 (glycoprotein L, gL), UL2 (uracil-DNA glycosylase), and UL3 (nuclear localizing phosphoprotein) of herpes simplex virus type 1 (HSV-1). Comparison of the deduced amino acid sequences of these three ORFs with HSV-1 counterparts revealed overall identities of 18, 43, and 49%, respectively. In spite of the low overall amino acid identity with HSV-1 gL, the first open reading frame was identified as a gL homolog of HSV-1 based not only on the gene arrangement but also on a limited amino acid conservation among gL homologs of alpha-herpesviruses. To characterize the expression of the MDV gL gene, an antiserum to a hydrophilic region of the gene expressed in a bacterial expression vector was produced. Immunoprecipitation with this antiserum revealed a 25,000-Da polypeptide in MDV-infected cells. Furthermore, the 25,000-Da polypeptide migrated as a 18,000-Da polypeptide following PNGase F treatment. This result is consistent with the predicted molecular weight of MDV gL, considering the two potential N-glycosylation sites and the predicted N-terminal signal sequence. A recombinant fowlpox virus expressing the MDV gL gene was generated to characterize this glycoprotein. Unlike gL in MDV-infected cells, gL expressed by recFPV-gL was highly sensitive to Endo H, indicating that it was probably retained in the endoplasmic reticulum and was not properly processed to a mature form. Therefore, similar to HSV-1 coexpression and complex formation of MDV gL and gH may be required for proper processing and transport of gL to the cell surface.
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PMID:Identification and characterization of a Marek's disease virus gene homologous to glycoprotein L of herpes simplex virus. 809 71

Dentin sialophosphoprotein (DSPP) is a major secretory product of odontoblasts and is critical for proper dentin formation. DSPP is believed to be processed into only two structural/functional domains: dentin sialoprotein (DSP) and dentin phosphoprotein (DPP). Here we report the isolation and characterization of a third domain of DSPP, designated dentin glycoprotein (DGP). DGP was isolated from a guanidine/EDTA extract of porcine tooth dentin by ion exchange, hydroxyapatite affinity, size exclusion, and RP-HPL chromatography. Endoproteinase lysine C digestion products of DGP were characterized by Edman sequencing and mass spectrometry. The porcine DGP backbone is the 81-amino acid segment of DSPP (Ser392 to Gly472) between the DSP and DPP domains. DGP has four phosphorylated serine residues (Ser453, Ser455, Ser457, and Ser462) and one glycosylated asparagine (Asn397). There are no other post-translational modifications. DGP is a stains-all positive protein with an apparent molecular mass on SDS-PAGE of 19 kDa, which is reduced by glycopeptidase A digestion to 16 kDa. A variety of glycans can be linked to Asn397. All are complex biantennary structures with a common N-linked pentasaccharide core (mannose3-N-acetylglucosamine2), most with a fucosyl residue on the innermost N-acetylglucosamine. The alpha1-3 and alpha1-6 arms are always galactose beta1-4 N-acetylglucosamine beta1-2 mannose, and either or both arms can be unsialidated or monosialidated. The calculated monoisotopic molecular masses of the different glycosylated forms of the DGP phosphoprotein are: unsialidated 10,523 and 10,670, monosialidated 10,815 and 10,961, and disialidated 11,106, and 11,252 Da, with the disialidated forms being the most abundant.
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PMID:Dentin glycoprotein: the protein in the middle of the dentin sialophosphoprotein chimera. 1572 77