Literature DB >> 3155519

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

P Fürst, M Solioz.   

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.

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Year:  1985        PMID: 3155519

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  3 in total

1.  ATP-dependent cadmium transport by the cadA cadmium resistance determinant in everted membrane vesicles of Bacillus subtilis.

Authors:  K J Tsai; K P Yoon; A R Lynn
Journal:  J Bacteriol       Date:  1992-01       Impact factor: 3.490

2.  Gene structure of Enterococcus hirae (Streptococcus faecalis) F1F0-ATPase, which functions as a regulator of cytoplasmic pH.

Authors:  C Shibata; T Ehara; K Tomura; K Igarashi; H Kobayashi
Journal:  J Bacteriol       Date:  1992-10       Impact factor: 3.490

3.  Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells.

Authors:  E J Bowman; A Siebers; K Altendorf
Journal:  Proc Natl Acad Sci U S A       Date:  1988-11       Impact factor: 11.205

  3 in total

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