Literature summary for 7.1.2.2 extracted from

Yagi, H.; Konno, H.; Murakami-Fuse, T.; Isu, A.; Oroguchi, T.; Akutsu, H.; Ikeguchi, M.; Hisabori, T.
Structural and functional analysis of the intrinsic inhibitor subunit epsilon of F1-ATPase from photosynthetic organisms (2010), Biochem. J., 425, 85-94.

Search for more literature for 7.1.2.2

Cloned(Commentary)

Cloned (Comment)	Organism
expression of the the cyano-epsilon, CF1-epsilon and the chimeric epsilon subunits in Escherichia coli strain BL21(DE3) as soluble proteins	Thermosynechococcus vestitus

Protein Variants

Protein Variants	Comment	Organism
additional information	inhibition of ATPase activity by the cyanobacterial epsilon subunit and the chimeric subunits composed of the N-terminal domain from the cyanobacterium and the C-terminal domain from spinach, overview	Thermosynechococcus vestitus

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	ATP synthase contains an intrinsic inhibitor subunit epsilon, that acts as an endogenous inhibitor of chloroplast F1-ATPase, structure-function analysis, overview. Inhibition of ATPase activity by the cyanobacterial epsilon subunit and the chimaeric subunits composed of the N-terminal domain from the cyanobacterium and the C-terminal domain from spinach, overview	Thermosynechococcus vestitus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
chloroplast membrane	-	Thermosynechococcus vestitus	31969	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Thermosynechococcus vestitus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ADP + phosphate + H+/out	Thermosynechococcus vestitus	the enzyme cannot synthesize ATP in the dark, but may catalyze futile ATP hydrolysis reactions	ATP + H2O + H+/in	-	r

Organism

Organism	UniProt	Comment	Textmining
Thermosynechococcus vestitus	-	strain BP-1	-

Renatured (Commentary)

Renatured (Comment)	Organism
denaturation of recombinant the cyano-epsilon, CF1-epsilon and the chimeric epsilon subunits, expressed from Escherichia coli strain BL21(DE3) as soluble proteins, using 8 M urea, and subsequent refolding	Thermosynechococcus vestitus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ADP + phosphate + H+/out	the enzyme cannot synthesize ATP in the dark, but may catalyze futile ATP hydrolysis reactions	Thermosynechococcus vestitus	ATP + H2O + H+/in	-	r
additional information	structure-function relationship of the intrinsic inhibitor subunit epsilon subunit in F1 from photosynthetic organism, overview	Thermosynechococcus vestitus	?	-	?

Subunits

Subunits	Comment	Organism
More	structure-function relationship of the intrinsic inhibitor subunit epsilon subunit in F1 from photosynthetic organism, NMR structure of the epsilon subunits, wild-type and mrecombinant/chimeric, overview. Analysis of the flexibility of the C-terminal domains using molecular dynamics simulations, overview	Thermosynechococcus vestitus

Synonyms

Synonyms	Comment	Organism
ATP synthase	-	Thermosynechococcus vestitus
F1-ATPase	-	Thermosynechococcus vestitus

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
additional information	-	additional information	rate constants of the epsilon-binding obtained from epsilon-inhibition, overview	Thermosynechococcus vestitus

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Release 2023.1 (January 2023)