Aminotransferases mutagenesis

J. J. Onuffer and J. F. Kirsch, Redesign of the substrate specificity of Escherichia cdi aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis, Protein Sci. 1995, 4, 1750-1757. 

Wu JY, Kao HJ, Li SC, Stevens R, Hillman S, Millington D, Chen YT. ENU mutagenesis identifies mice with mitochondrial branched-chain aminotransferase deficiency resembling human maple syrup urine disease. J. Clin. Invest. 2004 113 434 440. 

For aspartate aminotransferase, Lys-258 forms a Schiff base with PLP. Formation of the enzyme-substrate Schiff base rotates the coenzyme and places the a-hydrogen to be removed in the immediate vicinity of Lys-258, which is then responsible for proton transfer. Site-directed mutagenesis studies are also consis-... 

C.N. Cronin, B.A. Malcolm, J.F. Kirsch, Reversal of substrate charge specificity by site-directed mutagenesis of aspartate aminotransferase,/. Am. Chem. Soc. 1987, 109, 2222-2223. 

The most recent crystallographic study discloses the structure of the methylamine oxidase from the yeast Hansenula polymorpha [31], which shows an integrated network of water molecules providing electron transfer from topa quinone to copper and other important features such as the channel for oxygen entry and hydrogen peroxide release. The role of the active site aspartate base (Asp319) in the aminotransferase mechanism of the copper amine oxidase from H. polymorpha has been probed by site-directed mutagenesis [141]. It has been demonstrated by several... 

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