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2-Oxoacid:ferredoxin oxidoreductases (OFORs) are essential enzymes in microbial one-carbon metabolism. They use thiamine pyrophosphate to reversibly cleave carbon-carbon bonds, generating low potential (~-500 mV) electrons. Crystallographic analysis of a recently discovered OFOR, an oxalate oxidoreductase (OOR), has provided a second view of OFOR architecture and active site composition. Using these recent structural data along with the previously determined structures of pyruvate:ferredoxin oxidoreductase, structure-function relationships in this superfamily have been expanded and re-evaluated. Additionally, structural motifs have been defined that better serve to distinguish one OFOR subfamily from another and potentially uncover novel OFORs.

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DSpace at MIT  


Gibson, Marcus Ian -  Chen, Yang -  Ting -  Drennan, Catherine L. - 

Id.: 71476932

Versión: 1.0

Estado: Final

Tipo de recurso: Article  -  http://purl.org/eprint/type/JournalArticle  - 

Tipo de Interactividad: Expositivo

Nivel de Interactividad: muy bajo

Audiencia: Estudiante  -  Profesor  -  Autor  - 

Estructura: Atomic

Coste: no

Copyright: sí

: Creative Commons Attribution-NonCommercial-NoDerivs License

Requerimientos técnicos:  Browser: Any - 

Relación: [IsBasedOn] PMC
[References] http://dx.doi.org/10.1016/J.SBI.2016.05.011
[References] Current Opinion in Structural Biology

Fecha de contribución: 20-jun-2018


* 0959-440X
* Gibson, Marcus I et al. “A Structural Phylogeny for Understanding 2-Oxoacid Oxidoreductase Function.” Current Opinion in Structural Biology 41 (December 2016): 54–61 © 2016 Elsevier Ltd

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