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Trapping specific quaternary states of the allosteric enzyme aspartate transcarbamoylase in silica matrix sol-gels.
- Source :
-
Journal of the American Chemical Society [J Am Chem Soc] 2003 Aug 20; Vol. 125 (33), pp. 9924-5. - Publication Year :
- 2003
-
Abstract
- The extreme T and R quaternary structures of the allosteric enzyme aspartate transcarbamoylase have been trapped by encapsulation in a silica sol-gel matrix. Detection of the specific quaternary structure present in the sol-gel was accomplished using a pyrene-labeled version of the enzyme that exhibited monomer fluorescence in the T quaternary structure and excimer fluorescence in the R quaternary structure. Using thin films of the encapsulated enzyme, kinetics of the T and R states could be determined without interconversion of the states. Using a monolith form of the encapsulated enzyme, the transition from the T or the R structure was monitored. Within the sol-gel matrix, the rate of the transition was slowed approximately 105 over that observed in solution.
- Subjects :
- Aspartate Carbamoyltransferase antagonists & inhibitors
Aspartate Carbamoyltransferase metabolism
Binding Sites
Cytidine Triphosphate chemistry
Enzymes, Immobilized antagonists & inhibitors
Enzymes, Immobilized metabolism
Escherichia coli enzymology
Gels
Kinetics
Protein Conformation
Scattering, Radiation
Solutions
Spectrometry, Fluorescence
Uridine Triphosphate chemistry
X-Rays
Aspartate Carbamoyltransferase chemistry
Enzymes, Immobilized chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0002-7863
- Volume :
- 125
- Issue :
- 33
- Database :
- MEDLINE
- Journal :
- Journal of the American Chemical Society
- Publication Type :
- Academic Journal
- Accession number :
- 12914446
- Full Text :
- https://doi.org/10.1021/ja0360440