Contribution of Sequence Structure to the Thermotolerance of Tyrosine Phenol Lyase
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Abstract:
In order to understand the relationship between the thermostability of tyrosine phenol lyase (TPL) and its sequence, and to provide a reference for mutating the tyrosine phenol lyase to produce thermotolerant tyrosine phenol lyase, bioinformatics was used to analyze the thermostable tyrosine phenollyases, StTPL derived from Symbiobacterium toebii, FnTPL derived from Fusobacterium nucleatum, and mesophilic CfTPL derived from Citrobacter freundii. These lyases were compared in terms of phylogenetic tree, primary structure, secondary structure and tertiary structure. With the increase of the proline content in the primary structure of TPL, the optimal reaction temperature increased. The proline contents of StTPL, FnTPL and CfTPL were 5.02%, 3.70% and 2.85%, respectively. There were more β-sheets and turns in the secondary structure, which were 25.51%, 25.00%, and 23.91%, respectively. These characteristics were in line with the difference between thermostable enzymes and mesophilic enzymes reported in the literature. The comparison of the three-dimensional structures of StTPL, FnTPL and CfTPL revealed that the 310-313 residue region, residue 13, and 82-88 residue region had a poor superposition effect. The mutation of the 313 residue was conducive to the thermalstability of CfTPL. The mutation ofAla13, Glu83 and Thr407 residue was conducive to the thermalstability of StTPL. It is speculated that the above residue regions are related to thermalstability, which is also in line with the findings reported in the literature. In addition, the relevant bioinformatics analysis provides a preliminary reference for further understanding the hyperstability mechanism of hyperstable enzymes and screening and transforming new hyperstable enzymes.
