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  Local changes in the catalytic site of mammalian histidine decarboxylase can affect its global conformation and stability

Rodriguez-Caso, C., Rodriguez-Agudo, D., Moya-Garcia, A. A., Fajardo, I., Medina, M. A., Subramaniam, V., et al. (2003). Local changes in the catalytic site of mammalian histidine decarboxylase can affect its global conformation and stability. European Journal of Biochemistry, 270, 4376-4387. Retrieved from http://www3.interscience.wiley.com/cgi-bin/fulltext/118830151/PDFSTART.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F1CE-1 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-E401-4
Genre: Journal Article

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 Creators:
Rodriguez-Caso, C., Author
Rodriguez-Agudo, D., Author
Moya-Garcia, A. A., Author
Fajardo, I., Author
Medina, M. A., Author
Subramaniam, V.1, Author              
Sanchez-Jimenez, F., Author
Affiliations:
1Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society, ou_578628              

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Free keywords: histidine decarboxylase; histamine; a-fluoromethylhistidine; L-histidine methyl ester; pyridoxal phosphate-dependent enzymes.
 Abstract: Mature, active mammalian histidine decarboxylase is a dimeric enzyme of carboxy-truncated monomers ( ~53 kDa). By using a biocomputational approach, we have generated a three-dimensional model of a recombinant 1/512 fragment of the rat enzyme, which shows kinetic constants similar to those of the mature enzyme purified from rodent tissues. This model, together with previous spectroscopic data, allowed us to postulate that the occupation of the catalytic center by the natural substrate, or by substrate-analogs, would induce remarkable changes in the conformation of the intact holoenzyme.To investigate the proposed conformational changes during catalysis, we have carried out electrophoretic, chromatographic and spectroscopic analyses of purified recombinant rat 1/512 histidine decarboxylase in the presence of the natural substrate or substrate-analogs. Our results suggest that local changes in the catalytic site indeed affect the global conformation and stability of the dimeric protein.These results provide insights for new alternatives to inhibit histamine production efficiently in vivo.

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Language(s): eng - English
 Dates: 2003
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

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Title: European Journal of Biochemistry
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 270 Sequence Number: - Start / End Page: 4376 - 4387 Identifier: -