African Journal of
Biochemistry Research

  • Abbreviation: Afr. J. Biochem. Res.
  • Language: English
  • ISSN: 1996-0778
  • DOI: 10.5897/AJBR
  • Start Year: 2007
  • Published Articles: 368

Full Length Research Paper

Investigating structure-activity relationships within Enterococcus faecalis 2-deoxyribose aldolase

Nathan Wymer*, Jeremy Steflik and Maria Brown
Pfizer Global Research and Development, Groton, Connecticut (CT), USA.
Email: [email protected]

  • Article Number - 5D1886512458
  • Vol.5(6), pp. 172-175, June 2011
  •  Accepted: 17 May 2011
  •  Published: 30 June 2011

Abstract

The 2-deoxyribose aldolase (DERA) is an enzyme used for the synthesis and decomposition of carbohydrates. The DERA has been shown in previous studies to be utilized in an alternative metabolic pathway during stress. This article uses the Enterococcus faecalis DERA as a model system to study the structure-function relationship of amino acids towards DERA activity in hopes of garnering a better understanding of catalytic activity and possible mutations outside the binding pocket that might affect this activity. The active site was probed using saturation mutagenesis and identified two positions that increased activity (His187, Ser206). The outer shell amino acids were selected using bioinformatics. Mutagenesis of these outer shell amino acids combined with statistical analysis identified whether mutation of amino acids were advantageous or deleterious towards overall DERA activity without the need for high-throughput screening. These results will provide a basis to further study the intricate structure-activity relationships of amino acids within this DERA.

 

Key words: Enterococcus faecalis, 2-deoxyribose aldolase, structure-function relationships.

Abbreviation

DERA, 2-Deoxyribose aldolase; G3P, glyceraldehyde-3-phosphate; TB, terrific broth.

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