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16. Aldose Reductase from Pig Lens

Author

Tête-Favier, F., primary, Mitchler, A., additional, Podjarny, A.D., additional, Moras, D., additional, Barth, P., additional, Rondeau, J.-M., additional, Urzhumtsev, A., additional, and Biellmann, J.-F., additional

Published
1995
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22. General discussion.

Author

McQuillin, F. J., Bond, G. C., Biellmann, J. F., Ugo, R., James, B. R., Williams, R. J. P., Webster, D. E., Halpern, J., Gillard, R. D., Wells, P. B., Candlin, J. P., Oldham, A. R., Pratt, J. M., and Simándi, L. I.

Published
1968
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23. De l'origine du pic [M - 1] dans le spectre de masse de la N,N-diméthylbenzamide.

Author

Biellmann, J. F. and Hirth, C. G.

Abstract

Copyright of Organic Mass Spectrometry is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Published
1969
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25. X-ray analysis of D-xylose isomerase at 1.9 A: native enzyme in complex with substrate and with a mechanism-designed inactivator.

Author

Carrell, H L, Glusker, J P, Burger, V, Manfre, F, Tritsch, D, and Biellmann, J F

Abstract

The structures of crystalline D-xylose isomerase (D-xylose ketol-isomerase; EC 5.3.1.5) from Streptomyces rubiginosus and of its complexes with substrate and with an active-site-directed inhibitor have been determined by x-ray diffraction techniques and refined to 1.9-A resolution. This study identifies the active site, as well as two metal-binding sites. The metal ions are important in maintaining the structure of the active-site region and one of them binds C3-O and C5-O of the substrate forming a six-membered ring. This study has revealed a very close contact between histidine and C1 of a substrate, suggesting that this is the active-site base that abstracts a proton from substrate. The mechanism-based inhibitor is a substrate analog and is turned over by the enzyme to give a product that alkylates this same histidine, reinforcing our interpretation. The changes in structure of the native enzyme, the enzyme with bound substrate, and the alkylated enzyme indicate that the mechanism involves an "open-chain" conformation of substrate and that the intermediate in the isomerization reaction is probably a cis-ene diol because the active-site histidine is correctly placed to abstract a proton from C1 or C2 of the substrate. A water molecule binds to C1O and C2O of the substrate and so may act as a proton donor or acceptor in the enolization of a ring-opened substrate.

Published
1989
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27. Synthesis of Nucleoside Dimers Bridged on Ribose with a Butadiynyl Group

Author

Jung, F., Burger, A., and Biellmann, J.-F.

Abstract

The nucleoside dimer linked by a butadiynediyl group at C-3‘β may serve as a building block for the preparation of backbone-modified oligonucleotides for DNA repair or mutation in functional genomics. We prepared this type of dimer by an Eglington or Sonogashira coupling reaction. The unsymmetrical dimer was synthesized by coupling the acetylene with the bromoacetylene. Only marginal cytotoxicity was detected for one of the dimers.

Published
2003

29. Aldose Reductase from pig lens

Author

Frederique Favier, Barth, P., Mitchler, A., Podjarny, A. D., Rondeau, J. -M, Urzhumtsev, A., Biellmann, J. -F, and Moras, D.

Subjects
Pharmacology, Organic Chemistry, Drug Discovery, General Medicine

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