Formation of a beta-aspartyl phosphate intermediate by the vanadate-sensitive ATPase of Streptococcus faecalis.
The vanadate-sensitive membrane ATPase of Streptococcus faecalis forms, as part of the reaction cycle, an acylphosphate intermediate. The phosphorylated amino acid residue was identified by reducing the purified reconstituted phosphoenzyme with [3H]borohydride, followed by acid hydrolysis of the protein and quantitative amino acid analysis. Tritiated homoserine was found to be the resulting reaction product, generated through the reduction of a beta-aspartyl phosphate residue. The S. faecalis ATPase thus forms the same phosphorylated intermediate as a number of eukaryotic transport ATPases and appears to be related to these enzymes.
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D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D001224:Aspartic Acid / Q000031:analogs & derivatives* / Q000032:analysis; D013293:Enterococcus faecalis / Q000201:enzymology*; D010766:Phosphorylation; D014638:Vanadates; D014639:Vanadium / Q000494:pharmacology*
D000596:Amino Acids; D014639:Vanadium; C032197:beta-aspartyl phosphate; D001224:Aspartic Acid; D014638:Vanadates; D000251:Adenosine Triphosphatases