Literature summary for 7.1.1.1 extracted from

Oswald, C.; Johansson, T.; Tornroth, S.; Okvist, M.; Krengel, U.
Crystallization and preliminary crystallographic analysis of the NAD(H)-binding domain of Escherichia coli transhydrogenase (2004), Acta Crystallogr. Sect. D, 60, 743-745.

Search for more literature for 7.1.1.1

Cloned(Commentary)

Cloned (Comment)	Organism
domain dI expressed in Escherichia coli	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
dimers of dI domains using hanging-drop vapor diffusion method	Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	-	Escherichia coli	16020	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
NADH + NADP+	Escherichia coli	links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, cellular regeneration of NADPH	NAD+ + NADPH	-	r

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant protein	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
NADH + NADP+	-	Escherichia coli	NAD+ + NADPH	-	r
NADH + NADP+	links hydride transfer between NAD(H) and NADP(H) to the translocation of protons across membrane, cellular regeneration of NADPH	Escherichia coli	NAD+ + NADPH	-	r

Subunits

Subunits	Comment	Organism
dimer	isolated dI domains	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
NAD(P)+	-	Escherichia coli
NAD(P)H	-	Escherichia coli

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Release 2023.1 (January 2023)