3gch

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{{STRUCTURE_3gch| PDB=3gch | SCENE= }}
{{STRUCTURE_3gch| PDB=3gch | SCENE= }}
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'''CHEMISTRY OF CAGED ENZYMES. BINDING OF PHOTOREVERSIBLE CINNAMATES TO CHYMOTRYPSIN'''
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===CHEMISTRY OF CAGED ENZYMES. BINDING OF PHOTOREVERSIBLE CINNAMATES TO CHYMOTRYPSIN===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 2364065 is the PubMed ID number.
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{{ABSTRACT_PUBMED_2364065}}
==About this Structure==
==About this Structure==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/2364065 2364065]
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:[http://www.ncbi.nlm.nih.gov/pubmed/2364065 2364065]
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Photolysis and deacylation of inhibited chymotrypsin., Stoddard BL, Bruhnke J, Koenigs P, Porter N, Ringe D, Petsko GA, Biochemistry. 1990 Sep 4;29(35):8042-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2261462 2261462]
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Structure of chymotrypsin-trifluoromethyl ketone inhibitor complexes: comparison of slowly and rapidly equilibrating inhibitors., Brady K, Wei AZ, Ringe D, Abeles RH, Biochemistry. 1990 Aug 21;29(33):7600-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2271520 2271520]
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Inhibition of chymotrypsin by peptidyl trifluoromethyl ketones: determinants of slow-binding kinetics., Brady K, Abeles RH, Biochemistry. 1990 Aug 21;29(33):7608-17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2271521 2271521]
[[Category: Chymotrypsin]]
[[Category: Chymotrypsin]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Ringe, D.]]
[[Category: Ringe, D.]]
[[Category: Stoddard, B L.]]
[[Category: Stoddard, B L.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:28:42 2008''

Revision as of 09:28, 27 July 2008

Image:3gch.png

Template:STRUCTURE 3gch

CHEMISTRY OF CAGED ENZYMES. BINDING OF PHOTOREVERSIBLE CINNAMATES TO CHYMOTRYPSIN

Template:ABSTRACT PUBMED 2364065

About this Structure

3GCH is a Single protein structure. 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

Photolysis and deacylation of inhibited chymotrypsin., Stoddard BL, Bruhnke J, Koenigs P, Porter N, Ringe D, Petsko GA, Biochemistry. 1990 Sep 4;29(35):8042-51. PMID:2261462

Structure of chymotrypsin-trifluoromethyl ketone inhibitor complexes: comparison of slowly and rapidly equilibrating inhibitors., Brady K, Wei AZ, Ringe D, Abeles RH, Biochemistry. 1990 Aug 21;29(33):7600-7. PMID:2271520

Inhibition of chymotrypsin by peptidyl trifluoromethyl ketones: determinants of slow-binding kinetics., Brady K, Abeles RH, Biochemistry. 1990 Aug 21;29(33):7608-17. PMID:2271521

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