5.1.3.14	D413K	enzyme with mutation in the putative kinase active site shows drastic loss in their kinase activity but retains their epimerase activity	641739	
5.1.3.14	D413N	enzyme with mutation in the putative kinase active site shows drastic loss in their kinase activity but retains their epimerase activity	641739	
5.1.3.14	H110A	mutant enzyme shows a drastic loss of epimerase activity, oligomerization is significantly different from that of the wild-type enzyme,loss of epimerase activity can largely by attributed to incorrect protein folding	641739	
5.1.3.14	H132A	mutant enzyme shows a drastic loss of epimerase activity, oligomerization is significantly different from that of the wild-type enzyme, loss of epimerase activity can largely by attributed to incorrect protein folding	641739	
5.1.3.14	H155A	mutant enzyme forms mainly trimeric enzyme with small amounts of hexamer	641739	
5.1.3.14	H155A	mutant enzyme shows a drastic loss of epimerase activity, loss of epimerase activity can largely by attributed to incorrect protein folding	641739	
5.1.3.14	H157A	mutant enzyme forms mainly trimeric enzyme with small amounts of hexamer	641739	
5.1.3.14	H157A	mutant enzyme shows a drastic loss of epimerase activity, loss of epimerase activity can largely by attributed to incorrect protein folding	641739	
5.1.3.14	H45A	mutant enzyme shows a drastic loss of epimerase activity	641739	
5.1.3.14	R420M	enzyme with mutation in the putative kinase active site shows drastic loss in their kinase activity but retains their epimerase activity	641739