Description
Amino acids are among the most important molecules in nature and chemistry since they play central roles both as intermediates in metabolism and as building blocks of proteins and pharmaceuticals. In living organisms enzymes that depend on pyridoxal-5’-phosphate (PLP) catalyze a wide variety of biochemical reactions involving amino acids substrates and their analogs. These enzymes have been exploited by chemists for the biocatalytic synthesis of natural amino acids, and most recently have been investigated for the asymmetric synthesis of non-canonical amino acids. The high specificity towards natural substrates and sometimes low stereoselectivity is the limiting factor for the use of the PLP-dependent lyases in organic synthesis. Rational design represents an efficient approach for engineering of enzymes with desired properties. However, identification of functional residues is challenging, especially when structure-function relationships in an enzyme is poorly understood. Looking back to the evolution of enzymes within one family of PLP-dependent enzymes we want to understand how functionalities were evolved by Nature. In our project we compare the genetic and structural information of PLP-dependent enzymes using the bioinformatic tools in order to find the specific positions responsible for the catalytic diversity of this class of enzymes. The thorough investigation of the specific positions in the aminotransferase family of PLP-dependent enzymes assists to reveal the putative amino acid positions that mediate catalytic activity and substrate specificity in the L-threonine aldolase enzymes.| Period | 14 Nov 2016 → 16 Nov 2016 |
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| Event title | 1st European Summit of Industrial Biotechnology: esib 2016 |
| Event type | Conference |
| Location | Graz, Austria |
| Degree of Recognition | International |