Crystal Structures of Arginine Deiminase with Covalent Reaction Intermediates: Implications for Catalytic Mechanism
作者： Kalyan Das , Gary H Butler , Victoria Kwiatkowski , Arthur D Clark , Prem Yadav
DOI: 10.1016/J.STR.2004.02.017
关键词:
摘要: Arginine deiminase (ADI), an enzyme that hydrolyzes arginine to generate energy in many parasitic microorganisms, has potent anticancer activities and can halt growth of solid tumors. We determined the crystal structure ADI from Mycoplasma arginini two different forms (1.6 2.0 A resolution) using multiple isomorphous replacement. shares common structural features with arginine-catabolizing enzymes Arg:Gly amidinotransferase dimethylarginine dimethyl-aminohydrolase; contains additional domain five helices. The scissile C-N bonds substrates catalytic triads (Cys398-His269-Glu213 ADI) for three superimpose on each other. form I crystals corresponds a tetrahedral intermediate four heteroatoms (1S, 2N, 1O) covalently bonded reaction-center carbon. II represents amidino-enzyme complex; carbon is Cys398 sulfur nitrogens, reacting water molecule only 2.54 away.
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