-
cDNA cloning of porcine brain prolyl endopeptidase and identification of the active-site seryl residue.
Friedrich Miescher-Institut, Basel, Switzerland.
Prolyl endopeptidase is a cytoplasmic serine protease. The enzyme was purified from porcine kidney, and oligonucleotides based on peptide sequences from this protein were used to isolate a cDNA clone from a porcine brain library. This clone contained the complete coding sequence of prolyl endopeptidase and encoded a polypeptide with a molecular mass of 80,751 Da. The deduced amino acid sequence of prolyl endopeptidase showed no sequence homology with other known serine proteases. [3H]Diisopropyl fluorophosphate was used to identify the active-site serine of prolyl endopeptidase. One labeled peptide was isolated and sequenced. The sequence surrounding the active-site serine was Asn-Gly-Gly-Ser-Asn-Gly-Gly. This sequence is different from the active-site sequences of other known serine proteases. This difference and the lack of overall homology with the known families of serine proteases suggest that prolyl endopeptidase represents a new type of serine protease.
PMID: 1900195 [PubMed - indexed for MEDLINE]
-
Cited by 20 PubMed Central articles
-
Structural and mechanistic analysis of two prolyl endopeptidases: role of interdomain dynamics in catalysis and specificity.
Shan L, Mathews II, Khosla C.
Proc Natl Acad Sci U S A. 2005 Mar 8; 102(10):3599-604. Epub 2005 Feb 28.
[Proc Natl Acad Sci U S A. 2005]
-
Molecular, functional and structural properties of the prolyl oligopeptidase of Trypanosoma cruzi (POP Tc80), which is required for parasite entry into mammalian cells.
Bastos IM, Grellier P, Martins NF, Cadavid-Restrepo G, de Souza-Ault MR, Augustyns K, Teixeira AR, Schrével J, Maigret B, da Silveira JF, et al.
Biochem J. 2005 May 15; 388(Pt 1):29-38.
[Biochem J. 2005]
-
Comparative biochemical analysis of three bacterial prolyl endopeptidases: implications for coeliac sprue.
Shan L, Marti T, Sollid LM, Gray GM, Khosla C.
Biochem J. 2004 Oct 15; 383(Pt 2):311-8.
[Biochem J. 2004]
- » See all...