Molecular and Structural Discrimination of Proline Racemase and Hydroxyproline-2-Epimerase from Nosocomial and Bacterial Pathogens

Maira Goytia, Nathalie Chamond, Alain Cosson et al. · 2007

Read Molecular and Structural Discrimination of Proline Racemase and Hydroxyproline-2-Epimerase from Nosocomial and Bacterial Pathogens by Maira Goytia, Nathalie Chamond, Alain Cosson et al. (2007) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/plos-pone-0000885.txt.

Description

Maira Goytia, Nathalie Chamond, Alain Cosson and co-authors compared two closely related enzymes from harmful germs, in PLOS ONE in 2007. One enzyme, proline racemase, comes from the parasite that causes Chagas disease. It is a confirmed drug target because the parasite needs it to live and spread in its host.

The puzzle is that a near twin enzyme, hydroxyproline epimerase, does a slightly different job. Mixing the two up could mislead drug design. The team set out the molecular and structural marks that separate them. Clear marks like these help chemists aim at the parasite enzyme without hitting the wrong target.

Catalog record

CREATORMaira Goytia, Nathalie Chamond, Alain Cosson et al.
YEAR2007
COLLECTIONPAPERS
FORMATTXT
FILE SIZE41 KB
LICENSECreative Commons Attribution License
RIGHTSCC BY
SOURCEPLOS ONE

Source: https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0000885

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