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Bioinformatic analysis of a PLP-dependent enzyme superfamily suitable for biocatalytic applications
KTH, School of Biotechnology (BIO), Industrial Biotechnology. Greifswald University, Germany.
KTH, School of Biotechnology (BIO), Industrial Biotechnology.ORCID iD: 0000-0003-3073-5641
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2015 (English)In: Biotechnology Advances, ISSN 0734-9750, E-ISSN 1873-1899, Vol. 33, no 5, 566-604 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2015. Vol. 33, no 5, 566-604 p.
Keyword [en]
Annotation, Biocatalysis, Bioinformatics, Enzyme discovery, PLP-dependent enzymes, Protein function, Transaminase
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:kth:diva-162120DOI: 10.1016/j.biotechadv.2014.12.012ISI: 000358467500011PubMedID: 25575689ScopusID: 2-s2.0-84931009357OAI: diva2:797083
EU, FP7, Seventh Framework Programme, 289350

QC 20150827

Available from: 2015-03-22 Created: 2015-03-22 Last updated: 2015-08-27Bibliographically approved

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Steffen-Munsberg, FabianLand, HenrikBerglund, Per
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