Literature summary for 7.1.1.1 extracted from

Obiozo, U.M.; Brondijk, T.H.; White, A.J.; van Boxel, G.; Dafforn, T.R.; White, S.A.; Jackson, J.B.
Substitution of tyrosine 146 in the dI component of proton-translocating transhydrogenase leads to reversible dissociation of the active dimer into inactive monomers (2007), J. Biol. Chem., 282, 36434-36443.

Search for more literature for 7.1.1.1

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21(DE3) cells	Rhodospirillum rubrum

Protein Variants

Protein Variants	Comment	Organism
Y146A	mutation in component dI that binds NADH. dI.Y146A more readily dissociates into monomers than wild-type dI. dI.Y146A monomers bind NADH much more weakly than dimers. dI.Y146A reconstitutes activity to dI-depleted membranes in its dimeric form but not in its monomeric form	Rhodospirillum rubrum
Y146A	the mutant binds NADH much more weakly than the wild type enzyme	Rhodospirillum rubrum
Y146F	mutation in component dI that binds NADH. Wild-type dI and dI.Y146F reconstituted activity to dI-depleted membranes with similar characteristics	Rhodospirillum rubrum
Y146F	the mutant shows wild type NADH binding ability	Rhodospirillum rubrum

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	-	Rhodospirillum rubrum	16020	-

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
40300	-	2 * 40300, calculated from amino acid sequence	Rhodospirillum rubrum
84000	-	gel filtration	Rhodospirillum rubrum

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
NADPH + NAD+ + H+[side 1]	Rhodospirillum rubrum	-	NADP+ + NADH + H+[side 2]	-	?

Organism

Organism	UniProt	Comment	Textmining
Rhodospirillum rubrum	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
NADPH + NAD+ + H+[side 1]	-	Rhodospirillum rubrum	NADP+ + NADH + H+[side 2]	-	?
NADPH + oxidized acetyl pyridine adenine dinucleotide + H+[side 1]	-	Rhodospirillum rubrum	NADP+ + reduced acetyl pyridine adenine dinucleotide + H+[side 2]	-	r

Subunits

Subunits	Comment	Organism
dimer	2 * 40300, calculated from amino acid sequence	Rhodospirillum rubrum
More	the protein has three components: dI binds NADH, dIII binds NADP+, and dII spans the membrane. Transhydrogenase is a dimer of two dI-dII-dIII monomers. The two catalytic sites alternate during turnover	Rhodospirillum rubrum

Synonyms

Synonyms	Comment	Organism
proton-translocating transhydrogenase	-	Rhodospirillum rubrum
transhydrogenase	-	Rhodospirillum rubrum

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
-15	-	the enzyme remains stable for more than 3 months at -15°C	Rhodospirillum rubrum
4	-	the enzyme remains stable for more than 2 days at 4°C	Rhodospirillum rubrum

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Release 2023.1 (January 2023)