Cloning and sequence analysis of the gene encoding human lymphocyte prolyl endopeptidase
| Autor: | Filip Goossens, Dirk Hendriks, Simon Scharpé, G. Vriend, C. Van Broeckhoven, I. De Meester, G. Vanhoof, L. Hendriks |
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| Rok vydání: | 1994 |
| Předmět: |
Cytoplasm
Swine Sequence analysis Molecular Sequence Data education Biology Polymerase Chain Reaction Open Reading Frames chemistry.chemical_compound Prolyl endopeptidase Complementary DNA Escherichia coli Genetics medicine Animals Humans Amino Acid Sequence Lymphocytes Cloning Molecular Gene DNA Primers Bacteria Base Sequence Sequence Homology Amino Acid cDNA library Serine Endopeptidases Protein primary structure Brain Hominidae General Medicine Molecular biology Open reading frame Biochemistry chemistry cardiovascular system Prolyl Oligopeptidases DNA medicine.drug |
| Zdroj: | Gene |
| ISSN: | 0378-1119 |
| Popis: | The human cDNA encoding prolyl endopeptidase, a cytoplasmic endoprotease which hydrolyses the peptide bond at the C-terminal side of proline, was sequenced. After the isolation of the 3′ terminal fragment of the pep cDNA sequence from a human lymphocyte cDNA library, an approach based on the polymerase chain reaction (PCR) was undertaken to obtain the complete pep cDNA. Overlapping DNA fragments were generated by PCR from cDNA synthesized from human lymphocyte mRNA. The DNA fragments were subcloned and sequenced. The complete cDNA is 2562 nucleotides (nt) in length and contains an open reading frame coding for a protein of 710 amino acids (aa). Comparison of the primary PEP sequences from human lymphocyte and pig brain shows 97% identity. The aa sequence analysis shows homology with bacterial PEPs and with protease II from Escherichia coli. Asp641 probably participates in the active site of PEP. |
| Databáze: | OpenAIRE |
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