PMID:2838275
| Citation |
Bethell, RC and Lowe, G (1988) The stereochemical course of D-glyceraldehyde-induced ATPase activity of glycerokinase from Escherichia coli. Eur. J. Biochem. 174:387-9 |
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| Abstract |
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. |
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| Keywords |
Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/analogs & derivatives; Adenosine Triphosphate/metabolism; Catalysis; Chemical Phenomena; Chemistry; Enzyme Induction/drug effects; Escherichia coli/enzymology; Glyceraldehyde/pharmacology; Glycerol Kinase/metabolism; Hydrolysis; Oxygen Isotopes; Phosphofructokinase-1/metabolism; Phosphorylation; Phosphotransferases/metabolism; Stereoisomerism |
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