1o6f
From Proteopedia
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| - | [[Image:1o6f.jpg|left|200px]] | + | [[Image:1o6f.jpg|left|200px]] |
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| - | '''PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, D641A MUTANT WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO''' | + | {{Structure |
| + | |PDB= 1o6f |SIZE=350|CAPTION= <scene name='initialview01'>1o6f</scene>, resolution 1.6Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Prolyl_oligopeptidase Prolyl oligopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, D641A MUTANT WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1O6F is a [ | + | 1O6F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6F OCA]. |
==Reference== | ==Reference== | ||
| - | Substrate-dependent competency of the catalytic triad of prolyl oligopeptidase., Szeltner Z, Rea D, Juhasz T, Renner V, Mucsi Z, Orosz G, Fulop V, Polgar L, J Biol Chem. 2002 Nov 22;277(47):44597-605. Epub 2002 Sep 11. PMID:[http:// | + | Substrate-dependent competency of the catalytic triad of prolyl oligopeptidase., Szeltner Z, Rea D, Juhasz T, Renner V, Mucsi Z, Orosz G, Fulop V, Polgar L, J Biol Chem. 2002 Nov 22;277(47):44597-605. Epub 2002 Sep 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12228249 12228249] |
[[Category: Prolyl oligopeptidase]] | [[Category: Prolyl oligopeptidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: prolyl oligopeptidase]] | [[Category: prolyl oligopeptidase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:06:23 2008'' |
Revision as of 11:06, 20 March 2008
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| , resolution 1.6Å | |||||||
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| Sites: | |||||||
| Ligands: | and | ||||||
| Activity: | Prolyl oligopeptidase, with EC number 3.4.21.26 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, D641A MUTANT WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO
Overview
Prolyl oligopeptidase, a serine peptidase unrelated to trypsin and subtilisin, is implicated in memory disorders and is an important target of drug design. The catalytic competence of the Asp(641) residue of the catalytic triad (Ser(554), Asp(641), His(680)) was studied using the D641N and D641A variants of the enzyme. Both variants displayed 3 orders of magnitude reduction in k(cat)/K(m) for benzyloxycarbonyl-Gly-Pro-2-naphthylamide. Using an octapeptide substrate, the decrease was 6 orders of magnitude, whereas with Z-Gly-Pro-4-nitrophenyl ester there was virtually no change in k(cat)/K(m). This indicates that the contribution of Asp(641) is very much dependent on the substrate-leaving group, which was not the case for the classic serine peptidase, trypsin. The rate constant for benzyloxycarbonyl-Gly-Pro-thiobenzylester conformed to this series as demonstrated by a method designed for monitoring the hydrolysis of thiolesters in the presence of thiol groups. Alkylation of His(680) with Z-Gly-Pro-CH(2)Cl was concluded with similar rate constants for wild-type and D641A variant. However, kinetic measurements with Z-Gly-Pro-OH, a product-like inhibitor, indicated that the His(680) is not accessible in the enzyme variants. Crystal structure determination of these mutants revealed subtle perturbations related to the catalytic activity. Many of these observations show differences in the catalysis between trypsin and prolyl oligopeptidase.
About this Structure
1O6F is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Substrate-dependent competency of the catalytic triad of prolyl oligopeptidase., Szeltner Z, Rea D, Juhasz T, Renner V, Mucsi Z, Orosz G, Fulop V, Polgar L, J Biol Chem. 2002 Nov 22;277(47):44597-605. Epub 2002 Sep 11. PMID:12228249
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