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  Crystal structure and putative mechanism of 3-methylitaconate Δ-isomerase from Eubacterium barkeri.

Velarde, M., Macieira, S., Hilberg, M., Bröker, M., Tu, M. S., Golding, B. T., et al. (2009). Crystal structure and putative mechanism of 3-methylitaconate Δ-isomerase from Eubacterium barkeri. Journal of Molecular Biology, 391, 609-620.

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 Creators:
Velarde, M., Author
Macieira, S., Author
Hilberg, M., Author
Bröker, M., Author
Tu, M. S., Author
Golding, B. T., Author
Pierik, A. J.., Author
Buckel, W.1, Author           
Messerschmidt, A., Author
Affiliations:
1Max Planck Fellow Mechanism of Enzymes from Anaerobic Bacteria, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266319              

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Language(s): eng - English
 Dates: 2009
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 463896
 Degree: -

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Title: Journal of Molecular Biology
  Alternative Title : J. Mol. Biol.
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 391 Sequence Number: - Start / End Page: 609 - 620 Identifier: -