4.1.2.38	A28S	mutant shows decarboxylase activity towards 2-keto acids	678578	
4.1.2.38	A28S	point mutation converts BAL into a true benzoylformate decarboxylase. Km value for (R)-benzoin is virtually identical to that of the wild-type enzyme but whose kcat value is reduced ca. 10fold. Can decarboxylate benzoylformate, has a substrate spectrum comparable to that of benzoylformate decarboxylase, albeit with reduced activity. Methyl benzoylphosphonate and benzoylphosphonate act as competitive inhibitors in a time- and concentration-dependent manner	704205	
4.1.2.38	A480I	reduced lyase activity	678578	
4.1.2.38	F484I	reduced lyase activity	678578	
4.1.2.38	H286A	reduced lyase activity	678578	
4.1.2.38	H29A	the mutant shows 2.7% of wild type activity	747990	
4.1.2.38	H29A	the role of His29 in cofactor activation and catalysis is delineated	690982	
4.1.2.38	Q112A/E393A/S416G/T479A	variant with larger but less polar binding site	-, 762916	
4.1.2.38	Q112L/E393Y/S416G/T479F	variant with binding site matched to Pseudomonas fluorescens enzyme	-, 762916	
4.1.2.38	W163A	the role of Trp163 in cofactor activation and catalysis is delineated	690982