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PMID: 3155519 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Formation of a beta-aspartyl phosphate intermediate by the vanadate-sensitive ATPase of Streptococcus faecalis.

The Journal of biological chemistry ·Vol. 260 ·No. 1 ·1985-01-10 ·Pages 50-2

Fürst P, Solioz M

Abstract

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.

MeSH Terms
Adenosine Triphosphatases/metabolism Amino Acids/analysis Aspartic Acid/analogs & derivatives,analysis Enterococcus faecalis/enzymology Phosphorylation Vanadates Vanadium/pharmacology
Chemicals
Amino Acids Vanadium beta-aspartyl phosphate Aspartic Acid Vanadates Adenosine Triphosphatases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Fürst P
Solioz M
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1985-01-10
Pages
50-2
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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