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Literature summary for 7.4.2.8 extracted from

  • Rule, C.S.; Patrick, M.; Sandkvist, M.
    Measuring in vitro ATPase activity for enzymatic characterization (2016), J. Vis. Exp., 114, e54305 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
cardiolipin stimulates, K417 and K419 contribute to EpsE's ability to be stimulated by cardiolipin Vibrio cholerae serotype O1

Protein Variants

Protein Variants Comment Organism
K417A/K419A site-directed mutagenesis, the double lysine mutation in the EpsE zinc-binding domain highly reduces stimulated ATPase activity compared to wild-type by reducing the stimulation through cardiolipin Vibrio cholerae serotype O1

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Vibrio cholerae serotype O1
Zn2+ required, residues K417 and K419 are in volved in zinc binding Vibrio cholerae serotype O1

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Vibrio cholerae serotype O1
-
ADP + phosphate
-
?
ATP + H2O Vibrio cholerae serotype O1 El Tor Inaba N16961
-
ADP + phosphate
-
?
ATP + H2O Vibrio cholerae serotype O1 ATCC 39315
-
ADP + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Vibrio cholerae serotype O1 P37093
-
-
Vibrio cholerae serotype O1 ATCC 39315 P37093
-
-
Vibrio cholerae serotype O1 El Tor Inaba N16961 P37093
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
Vibrio cholerae serotype O1 ADP + phosphate
-
?
ATP + H2O
-
Vibrio cholerae serotype O1 El Tor Inaba N16961 ADP + phosphate
-
?
ATP + H2O
-
Vibrio cholerae serotype O1 ATCC 39315 ADP + phosphate
-
?
additional information basic assay developemnt for quantitatively measuring the in vitro activity of purified ATPases for functional characterization by detecting free phosphate through biding of malachite green molybdate, in vitro activity of the T2S ATPase EpsE can be stimulated by copurification of EpsE with the cytoplasmic domain of EpsL (EpsE-cytoEpsL) and addition of the acidic phospholipid cardiolipin. The assay consists of only one phosphate release measurement step, is highly sensitive, and can typically be performed within a few hours Vibrio cholerae serotype O1 ?
-
-
additional information basic assay developemnt for quantitatively measuring the in vitro activity of purified ATPases for functional characterization by detecting free phosphate through biding of malachite green molybdate, in vitro activity of the T2S ATPase EpsE can be stimulated by copurification of EpsE with the cytoplasmic domain of EpsL (EpsE-cytoEpsL) and addition of the acidic phospholipid cardiolipin. The assay consists of only one phosphate release measurement step, is highly sensitive, and can typically be performed within a few hours Vibrio cholerae serotype O1 El Tor Inaba N16961 ?
-
-
additional information basic assay developemnt for quantitatively measuring the in vitro activity of purified ATPases for functional characterization by detecting free phosphate through biding of malachite green molybdate, in vitro activity of the T2S ATPase EpsE can be stimulated by copurification of EpsE with the cytoplasmic domain of EpsL (EpsE-cytoEpsL) and addition of the acidic phospholipid cardiolipin. The assay consists of only one phosphate release measurement step, is highly sensitive, and can typically be performed within a few hours Vibrio cholerae serotype O1 ATCC 39315 ?
-
-

Synonyms

Synonyms Comment Organism
AAA+ ATPase
-
Vibrio cholerae serotype O1
adenosine triphosphate-hydrolyzing enzyme
-
Vibrio cholerae serotype O1
EpsE
-
Vibrio cholerae serotype O1

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Vibrio cholerae serotype O1

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
assay at Vibrio cholerae serotype O1

General Information

General Information Comment Organism
evolution EpsE is a AAA+ ATPase and member of the bacterial Type II/IV secretion subfamily of NTPases Vibrio cholerae serotype O1
additional information enzyme residues K417 and K419 do not contribute to EpsE's basal activity but rather to the ability of the protein to be stimulated by cardiolipin Vibrio cholerae serotype O1
physiological function adenosine triphosphate-hydrolyzing enzymes, or ATPases, play a critical role in a diverse array of cellular functions. These dynamic proteins can generate energy for mechanical work, such as protein trafficking and degradation, solute transport, and cellular movements. EpsE powers type II secretion (T2S) in Vibrio cholerae, the causative agent of cholera. The T2S system is responsible for the secretion of a wide variety of proteins Vibrio cholerae serotype O1