Publication Date:
1984-08-31
Description:
High-resolution carbon-13 nuclear magnetic resonance (NMR) spectra of enzyme-inhibitor and enzyme-substrate complexes provide detailed structural and stereochemical information on the mechanism of enzyme action. The proteases trypsin and papain are shown to form tetrahedrally coordinated complexes and acyl derivatives with a variety of compounds artificially enriched at the site or sites of interest. These results are compared with the structural information derived from x-ray diffraction. Detailed NMR studies have provided a clearer picture of the ionization state of the residues participating in enzyme-catalyzed processes than other more classical techniques. The dynamics of enzymic catalysis can be observed at sub-zero temperatures by a combination of cryoenzymology and carbon-13 NMR spectroscopy. With these powerful techniques, transient, covalently bound intermediates in enzyme-catalyzed reactions can be detected and their structures rigorously assigned.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mackenzie, N E -- Malthouse, J P -- Scott, A I -- New York, N.Y. -- Science. 1984 Aug 31;225(4665):883-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6433481" target="_blank"〉PubMed〈/a〉
Keywords:
Binding Sites
;
Carbon Isotopes
;
Carboxypeptidases/metabolism
;
Carboxypeptidases A
;
Catalysis
;
Chemical Phenomena
;
Chemistry
;
Coenzymes/*metabolism
;
Endopeptidases/metabolism
;
Enzymes/*metabolism
;
Freezing
;
Fructose-Bisphosphate Aldolase/metabolism
;
Magnetic Resonance Spectroscopy
;
Papain/metabolism
;
Pepsin A/metabolism
;
Peptide Hydrolases/*metabolism
;
Protease Inhibitors
;
Pterins/metabolism
;
Pyridoxal Phosphate/metabolism
;
Serine Endopeptidases
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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