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.
Dept. of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, Greifswald University, Felix-Hausdorff-Str. 4, 17487 Greifswald, Germany.
Biotechnol Adv. 2015 Sep-Oct;33(5):566-604. doi: 10.1016/j.biotechadv.2014.12.012. Epub 2015 Jan 7.
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.
在这篇综述中，我们分析了依赖 PLP 的酶超家族的结构/序列-功能关系，特别强调了 III 类转氨酶。胺转氨酶在生物催化合成手性胺方面的应用非常重要。此外，还讨论了其他酶活性，如外消旋酶或脱羧酶。底物范围和接受化学上不同类型底物的能力被证明反映在活性位点周围的保守氨基酸模式中。这些发现被浓缩在一个序列-功能矩阵中，这有助于注释和鉴定生物催化相关的酶，并对其进行蛋白质工程改造。
