A novel class of protease targets of phosphatidylethanolamine-binding proteins (PEBP): A study of the acylpeptide hydrolase and the PEBP inhibitor from the archaeon Sulfolobus solfataricus (446 views)
Mol Biosyst (ISSN: 1742-206x), 2010; 6(12): 2498-2507.
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Paper type: Journal Article,
Impact factor: 3.825, 5-year impact factor: 3.986
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-78149445520&partnerID=40&md5=01cd60e51bf58e7311f20af6182cfa4b
Keywords: Acylaminoacyl Peptidase, Acylaminoacyl-Peptidase, Peptide Hydrolase, Phosphatidylethanolamine Binding Protein, Proteinase Inhibitor, Amino Acid Sequence, Article, Chemical Structure, Chemistry, Drug Antagonism, Enzymology, Ic 50, Isolation And Purification, Kinetics, Metabolism, Molecular Genetics, Polyacrylamide Gel Electrophoresis, Protein Multimerization, Protein Transport, Sequence Alignment, Structural Homology, Sulfolobus Solfataricus, Inhibitory Concentration 50, Models, Molecular Sequence Data, Protease Inhibitors, Aeropyrum, Aeropyrum Pernix, Archaea, Mammalia, Pyrococcus Horikoshii,
Affiliations:
*** IBB - CNR ***
Institute of Protein Biochemistry, IBP-CNR, Napoli, Italy
Institute of Biostructures and Bioimaging, IBB-CNR, via Mezzocannone 16 80134, Napoli, Italy
Institute of Crystallography, IC-CNR, Bari, Italy
Department of Structural and Functional Biology, University of Naples Federico II, Napoli, Italy
References:
Not available.
Mol Biosyst (ISSN: 1742-206x), 2010; 6(12): 2498-2507.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.825, 5-year impact factor: 3.986
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-78149445520&partnerID=40&md5=01cd60e51bf58e7311f20af6182cfa4b
Keywords: Acylaminoacyl Peptidase, Acylaminoacyl-Peptidase, Peptide Hydrolase, Phosphatidylethanolamine Binding Protein, Proteinase Inhibitor, Amino Acid Sequence, Article, Chemical Structure, Chemistry, Drug Antagonism, Enzymology, Ic 50, Isolation And Purification, Kinetics, Metabolism, Molecular Genetics, Polyacrylamide Gel Electrophoresis, Protein Multimerization, Protein Transport, Sequence Alignment, Structural Homology, Sulfolobus Solfataricus, Inhibitory Concentration 50, Models, Molecular Sequence Data, Protease Inhibitors, Aeropyrum, Aeropyrum Pernix, Archaea, Mammalia, Pyrococcus Horikoshii,
Affiliations:
*** IBB - CNR ***
Institute of Protein Biochemistry, IBP-CNR, Napoli, Italy
Institute of Biostructures and Bioimaging, IBB-CNR, via Mezzocannone 16 80134, Napoli, Italy
Institute of Crystallography, IC-CNR, Bari, Italy
Department of Structural and Functional Biology, University of Naples Federico II, Napoli, Italy
References:
Not available.
A novel class of protease targets of phosphatidylethanolamine-binding proteins (PEBP): A study of the acylpeptide hydrolase and the PEBP inhibitor from the archaeon Sulfolobus solfataricus
This work describes the identification and characterization of a Sulfolobus solfataricus acylpeptide hydrolase, named APEHSs, recognised as a new protease target of the endogenous PEBP inhibitor, SsCEI. APEH is one of the four members of the prolyl oligopeptidase (POP) family, which removes acylated amino acid residues from the N terminus of oligopeptides. APEHSs is a cytosolic homodimeric protein with a molecular mass of 125 kDa. It displays a similar exopeptidase and endopeptidase activity to the homologous enzymes from Aeropyrum pernix and Pyrococcus horikoshii. Herein we demonstrate that SsCEI is the first PEBP protein found to efficiently inhibit APEH from both S. solfataricus and mammalian sources with IC50 values in the nanomolar range. The 3D model of APEHSs shows the typical structural features of the POP family including an N-terminal β-propeller and a C-terminal α/β hydrolase domain. Moreover, to gain insights into the binding mode of SsCEI toward APEHSs, a structural model of the inhibition complex is proposed, suggesting a mechanism of steric blockage on substrate access to the active site or on product release. Like other POP enzymes, APEH may constitute a new therapeutic target for the treatment of a number of pathologies and this study may represent a starting point for further medical research. © 2010 The Royal Society of Chemistry.
This work describes the identification and characterization of a Sulfolobus solfataricus acylpeptide hydrolase, named APEHSs, recognised as a new protease target of the endogenous PEBP inhibitor, SsCEI. APEH is one of the four members of the prolyl oligopeptidase (POP) family, which removes acylated amino acid residues from the N terminus of oligopeptides. APEHSs is a cytosolic homodimeric protein with a molecular mass of 125 kDa. It displays a similar exopeptidase and endopeptidase activity to the homologous enzymes from Aeropyrum pernix and Pyrococcus horikoshii. Herein we demonstrate that SsCEI is the first PEBP protein found to efficiently inhibit APEH from both S. solfataricus and mammalian sources with IC50 values in the nanomolar range. The 3D model of APEHSs shows the typical structural features of the POP family including an N-terminal β-propeller and a C-terminal α/β hydrolase domain. Moreover, to gain insights into the binding mode of SsCEI toward APEHSs, a structural model of the inhibition complex is proposed, suggesting a mechanism of steric blockage on substrate access to the active site or on product release. Like other POP enzymes, APEH may constitute a new therapeutic target for the treatment of a number of pathologies and this study may represent a starting point for further medical research. © 2010 The Royal Society of Chemistry.
A novel class of protease targets of phosphatidylethanolamine-binding proteins (PEBP): A study of the acylpeptide hydrolase and the PEBP inhibitor from the archaeon Sulfolobus solfataricus
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A novel class of protease targets of phosphatidylethanolamine-binding proteins (PEBP): A study of the acylpeptide hydrolase and the PEBP inhibitor from the archaeon Sulfolobus solfataricus
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View Export to BibTeX Export to EndNote
Grasso G, D'Agata R, Rizzarelli E, Spoto G, D'Andrea LD, Pedone C, Picardi A, Romanelli A, Fragai M, Yeo KJ
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Impact Factor: 3.574
View Export to BibTeX Export to EndNote
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Impact Factor: 3.922
View Export to BibTeX Export to EndNote
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Impact Factor: 5.873
View Export to BibTeX Export to EndNote
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Impact Factor: 7.258
View Export to BibTeX Export to EndNote
Lombardi A, De Simone G, Galdiero S, Staiano N, Nastri F, Pavone V
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Impact Factor: 2.331
View Export to BibTeX Export to EndNote
Pavone V, De Simone G, Nastri F, Galdiero S, Staiano N, Lombardi A, Pedone C
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Impact Factor: 2.636
View Export to BibTeX Export to EndNote
22 Records (21 excluding Abstracts).
Total impact factor: 81.942 (78.408 excluding Abstracts).
Total 5 year impact factor: 74.331 (70.316 excluding Abstracts).
Total impact factor: 81.942 (78.408 excluding Abstracts).
Total 5 year impact factor: 74.331 (70.316 excluding Abstracts).
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