The stereochemical course of nucleotidyl transfer catalyzed by ATP sulfurylase.
ATP sulfurylase catalyzes the synthesis of ATP from adenosine 5'-phosphosulfate and magnesium pyrophosphate with inversion of configuration at phosphorus. This implies an "in line" displacement mechanism in the ternary complex and effectively eliminates both an adjacent mechanism followed by pseudorotation and a double displacement mechanism involving an adenylyl-enzyme intermediate. The double displacement mechanism had been invoked previously to account for a number of observations, including the ability of the enzyme to catalyze the hydrolysis of MgATP to AMP and MgPPi, and the exchange of Mg32PPi into MgATP in the absence of sulfate.
D000249:Adenosine Monophosphate / Q000031:analogs & derivatives*; D000250:Adenosine Phosphosulfate / Q000096:biosynthesis*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D009682:Magnetic Resonance Spectroscopy; D009713:Nucleotidyltransferases / Q000378:metabolism*; D013237:Stereoisomerism; D013430:Sulfate Adenylyltransferase / Q000378:metabolism*
D000249:Adenosine Monophosphate; D000250:Adenosine Phosphosulfate; D009713:Nucleotidyltransferases; D013430:Sulfate Adenylyltransferase