2.1.3.9	K302A	site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme	
2.1.3.9	K302E	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme. The side-chain of Glu302 in the K302E mutant structure is well defined and anchored by hydrogen bonding interaction with the main-chain nitrogen atom of Arg298 and weakly hydrogen bonded to the main-chain nitrogen atom of Ser253	
2.1.3.9	K302R	site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme	
2.1.3.9	additional information	computer model of molecular dynamic