Topographical analysis of trypsin active site structure by means of the “inverse substrate” method
Author:
Publisher
Elsevier BV
Subject
Organic Chemistry,Drug Discovery,Molecular Biology,Biochemistry
Reference20 articles.
1. Proteolytic enzymes. 7. "Inverse substrates" for trypsin. Efficient enzymic hydrolysis of certain esters with a cationic center in the leaving group
2. A novel "induced-fit" phenomenon. Evidence for conformational changes closely associated with efficient hydrolysis of acyl trypsin
3. A Novel Chiral Microenvironmental Probe at the Active Site of Trypsin. Extrinsic Cotton Effects of Acyl-trypsin Possessing an Enantiomeric Pair of Chromophores
4. Specific spin-labeling at trypsin active site Application of ‘inverse substrate’ to the structural analysis of the active site
5. Biomimetic and Bioorganic Chemistry III;Tanizawa,1986
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1. Photoregulation of deacylation rate of acyl trypsin derived from photoresponsive inverse substrate;Bioorganic & Medicinal Chemistry Letters;2003-11
2. Comparative Study of the Active Site Caging of Serine Proteases: Thrombin and Factor Xa;Biochemistry;2002-01-18
3. Synthesis of 2′,5′-Dideoxy-adenosine-3′-monophosphate Derivatives as Allosteric Inhibitors of Adenylyl Cyclase;Nucleosides and Nucleotides;1995-08
4. Inverse substrates for trypsin and trypsin-like enzymes;Accounts of Chemical Research;1987-09-01
5. Comparison of Streptomyces griseus and bovine trypsin by active site analysis using fluorescent acyl groups;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1987-07
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