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

Fabian Steffen-Munsberg; Clare Vickers; Hannes Kohls; Henrik Land; Hendrik Mallin; Alberto Nobili; Lilly Skalden; Tom van den Bergh; Henk-Jan Joosten; Per Berglund; Matthias Höhne; Uwe T Bornscheuer

doi:10.1016/j.biotechadv.2014.12.012

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

Biotechnol Adv. 2015 Sep-Oct;33(5):566-604. doi: 10.1016/j.biotechadv.2014.12.012. Epub 2015 Jan 7.

Authors

Affiliations

¹ Dept. of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, Greifswald University, Felix-Hausdorff-Str. 4, 17487 Greifswald, Germany; KTH Royal Institute of Technology, School of Biotechnology, Division of Industrial Biotechnology, AlbaNova University Center, SE-106 91 Stockholm, Sweden.
² Dept. of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, Greifswald University, Felix-Hausdorff-Str. 4, 17487 Greifswald, Germany.
³ Dept. of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, Greifswald University, Felix-Hausdorff-Str. 4, 17487 Greifswald, Germany; Protein Biochemistry, Institute of Biochemistry, Greifswald University, Felix-Hausdorff-Str. 4, 17487 Greifswald, Germany.
⁴ KTH Royal Institute of Technology, School of Biotechnology, Division of Industrial Biotechnology, AlbaNova University Center, SE-106 91 Stockholm, Sweden.
⁵ Bio-Prodict, Nieuwe Marktstraat 54E, 6511 AA Nijmegen, The Netherlands.
⁶ Protein Biochemistry, Institute of Biochemistry, Greifswald University, Felix-Hausdorff-Str. 4, 17487 Greifswald, Germany. Electronic address: [email protected].
⁷ Dept. of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, Greifswald University, Felix-Hausdorff-Str. 4, 17487 Greifswald, Germany. Electronic address: [email protected].

PMID: 25575689
DOI: 10.1016/j.biotechadv.2014.12.012

Abstract

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 of amino acids around the active site. These findings are condensed in a sequence-function matrix, which facilitates annotation and identification of biocatalytically relevant enzymes and protein engineering thereof.

Keywords: Annotation; Biocatalysis; Bioinformatics; Enzyme discovery; PLP-dependent enzymes; Protein function; Transaminase.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Biocatalysis
Biotechnology*
Computational Biology*
Pyridoxal Phosphate / metabolism*
Transaminases*

Substances

Pyridoxal Phosphate
Transaminases