Bioinformatic analysis of a PLP-dependent enzyme superfamily suitable for biocatalytic applications.

@article{SteffenMunsberg2015BioinformaticAO,
  title={Bioinformatic analysis of a PLP-dependent enzyme superfamily suitable for biocatalytic applications.},
  author={Fabian Steffen-Munsberg and Clare Vickers and Hannes Kohls and Henrik Land and Hendrik Mallin and Alberto Nobili and Lilly Skalden and Tom van den Bergh and Henk-Jan Joosten and Per Berglund and Matthias H{\"o}hne and Uwe T Bornscheuer},
  journal={Biotechnology advances},
  year={2015},
  volume={33 5},
  pages={566-604}
}
In this review we analyse structure/sequence-function relationships for the superfamily of PLP-dependent enzymes with special emphasis on class III transaminases. Amine transaminases are highly important for applications in biocatalysis in the synthesis of chiral amines. In addition, other enzyme activities such as racemases or decarboxylases are also discussed. The substrate scope and the ability to accept chemically different types of substrates are shown to be reflected in conserved patterns… CONTINUE READING

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References

Publications referenced by this paper.
Showing 1-10 of 198 references

Direct evidence for a glutamate switch necessary for substrate recognition: crystal structures of lysine ε-aminotransferase (Rv3290c) from Mycobacterium tuberculosis H37Rv

SM Tripathi, R. Ramachandran
J Mol Biol • 2006
View 4 Excerpts
Highly Influenced

A large-scale evaluation of computational protein function prediction

P Radivojac, WT Clark, +3 authors A Sokolov
Nat Methods 2013;10:221-7 • 2013
View 5 Excerpts
Highly Influenced

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