1be8: Difference between revisions

Revision as of 18:57, 30 June 2008

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File:1be8.png

Template:STRUCTURE 1be8

TRANS-CINNAMOYL-SUBTILISIN IN WATERTRANS-CINNAMOYL-SUBTILISIN IN WATER

Template:ABSTRACT PUBMED 9789015

About this StructureAbout this Structure

1BE8 is a Single protein structure of sequence from Bacillus licheniformis. Full crystallographic information is available from OCA.

ReferenceReference

Comparison of x-ray crystal structures of an acyl-enzyme intermediate of subtilisin Carlsberg formed in anhydrous acetonitrile and in water., Schmitke JL, Stern LJ, Klibanov AM, Proc Natl Acad Sci U S A. 1998 Oct 27;95(22):12918-23. PMID:9789015

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+===TRANS-CINNAMOYL-SUBTILISIN IN WATER===
-==Overview==
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-The x-ray crystal structures of trans-cinnamoyl-subtilisin, an acyl-enzyme covalent intermediate of the serine protease subtilisin Carlsberg, have been determined to 2.2-A resolution in anhydrous acetonitrile and in water. The cinnamoyl-subtilisin structures are virtually identical in the two solvents. In addition, their enzyme portions are nearly indistinguishable from previously determined structures of the free enzyme in acetonitrile and in water; thus, acylation in either aqueous or nonaqueous solvent causes no appreciable conformational changes. However, the locations of bound solvent molecules in the active site of the acyl- and free enzyme forms in acetonitrile and in water are distinct. Such differences in the active site solvation may contribute to the observed variations in enzymatic activities. On prolonged exposure to organic solvent or removal of interstitial solvent from the crystal lattice, the channels within enzyme crystals are shown to collapse, leading to a drop in the number of active sites accessible to the substrate. The mechanistic and preparative implications of our findings for enzymatic catalysis in organic solvents are discussed.
+The line below this paragraph, {{ABSTRACT_PUBMED_9789015}}, adds the Publication Abstract to the page
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 [[Category: Organic solvent]]
 [[Category: Serine protease]]
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