The stereochemical course of D-glyceraldehyde-induced ATPase activity of glycerokinase from Escherichia coli.
D-Glyceraldehyde-induced hydrolysis of adenosine (R)-5'-[gamma-17O,18O,thio]triphosphate catalysed by glycerokinase from Escherichia coli gives inorganic [16O,17O,18O]thiophosphate with the (S)-configuration, showing that the reaction proceeds with inversion of configuration at phosphorus. This result provides powerful support for the chemically most plausible mechanism, namely, that the hydrate of D-glyceraldehyde is the effective substrate which after phosphorylation or thiophosphorylation eliminates inorganic phosphate or inorganic thiophosphate, respectively, with regeneration of D-glyceraldehyde.
Bethell
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Dyson Perrins Laboratory, University of Oxford, England.
Lowe
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D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000031:analogs & derivatives / Q000378:metabolism; D002384:Catalysis; D055598:Chemical Phenomena; D002621:Chemistry; D004790:Enzyme Induction / Q000187:drug effects; D004926:Escherichia coli / Q000201:enzymology*; D005985:Glyceraldehyde / Q000494:pharmacology*; D005991:Glycerol Kinase / Q000378:metabolism*; D006868:Hydrolysis; D010103:Oxygen Isotopes; D010732:Phosphofructokinase-1 / Q000378:metabolism; D010766:Phosphorylation; D010770:Phosphotransferases / Q000378:metabolism*; D013237:Stereoisomerism
D010103:Oxygen Isotopes; C022571:adenosine 5'-O-(3-thiotriphosphate); D005985:Glyceraldehyde; D000255:Adenosine Triphosphate; D010770:Phosphotransferases; D010732:Phosphofructokinase-1; D005991:Glycerol Kinase; D000251:Adenosine Triphosphatases