Literature DB >> 15198585

Conversion of aquifex aeolicus 3-deoxy-d-manno-octulosonate 8-phosphate synthase, a metalloenzyme, into a nonmetalloenzyme.

Jingjing Li1, Jing Wu, Angela S Fleischhacker, Ronald W Woodard.   

Abstract

The Aquifex aeolicus 3-deoxy-d-manno-octulosonate 8-phosphate synthase (KDO8PS), a class II metalloenzyme, is converted into an active nonmetalloenzyme by a single amino acid mutation, namely, C11N. The result may provide insight into the evolutionary link between the two KDO8PS classes as well as the potential role of the metal and/or asparagine in the catalytic mechanism.

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Year:  2004        PMID: 15198585     DOI: 10.1021/ja0480872

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN: 0002-7863            Impact factor:   15.419


  3 in total

1.  Common basis for the mechanism of metallo and non-metallo KDO8P synthases.

Authors:  Peng Tao; H Bernhard Schlegel; Domenico L Gatti
Journal:  J Inorg Biochem       Date:  2010-08-19       Impact factor: 4.155

2.  Structure of a metal-independent bacterial glycosyltransferase that catalyzes the synthesis of histo-blood group A antigen.

Authors:  Nethaji Thiyagarajan; Tram T K Pham; Brittany Stinson; Amit Sundriyal; Percy Tumbale; Michelle Lizotte-Waniewski; Keith Brew; K Ravi Acharya
Journal:  Sci Rep       Date:  2012-12-07       Impact factor: 4.379

3.  The contribution of coevolving residues to the stability of KDO8P synthase.

Authors:  Sharon H Ackerman; Domenico L Gatti
Journal:  PLoS One       Date:  2011-03-09       Impact factor: 3.240

  3 in total

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