期刊
BIOTECHNOLOGY ADVANCES
卷 33, 期 5, 页码 566-604出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.biotechadv.2014.12.012
关键词
Protein function; Annotation; PLP-dependent enzymes; Bioinformatics; Biocatalysis; Enzyme discovery; Transaminase
资金
- Fonds der Chemischen Industrie (Chemiefonds-Stipendium)
- Deutsche Bundesstiftung Umwelt [AZ29937]
- COST Action [CM1303]
- European Union [289350]
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. (C) 2015 Elsevier Inc. All rights reserved.
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