4gch
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(New page: 200px<br /><applet load="4gch" size="450" color="white" frame="true" align="right" spinBox="true" caption="4gch, resolution 1.9Å" /> '''STRUCTURE AND ACTIVIT...)
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Revision as of 17:29, 20 November 2007
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STRUCTURE AND ACTIVITY OF TWO PHOTOREVERSIBLE CINNAMATES BOUND TO CHYMOTRYPSIN
Overview
The serine protease gamma-chymotrypsin was covalently inhibited with two, different photoreversible cinnamate compounds, and the structures of the, resulting complexes were determined to 1.9-A resolution. The inhibitors, show different kinetics of binding, inhibition, and nonphotochemical, deacylation relative to each other in solution activity assays. The, crystal structures of the enzyme-cinnamate complexes show that both, compounds acylate serine 195 and that the two molecules are bound in, similar nonproductive conformations which have drastic effects on their, ability to turn over. Substitution of a diethylamino group on the para, position of the cinnamate ring causes a 1000-fold increase in the thermal, stability of the inhibitor toward hydrolysis and deacylation.
About this Structure
4GCH is a Protein complex structure of sequences from Bos taurus with DMC as ligand. Active as Chymotrypsin, with EC number 3.4.21.1 Full crystallographic information is available from OCA.
Reference
Structure and activity of two photoreversible cinnamates bound to chymotrypsin., Stoddard BL, Bruhnke J, Porter N, Ringe D, Petsko GA, Biochemistry. 1990 May 22;29(20):4871-9. PMID:2364065
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