Literature summary for 1.6.2.2 extracted from

You, C.; Liu, C.; Li, Y.; Jiang, P.; Ma, Q.
Structural and enzymatic analysis of the cytochrome b5 reductase domain of Ulva prolifera nitrate reductase (2018), Int. J. Biol. Macromol., 111, 1175-1182 .

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Ulva prolifera

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of the cytochrome b5 reductase domain. The N-terminal FAD-binding domain primarily consists of six antiparallel beta-strands, a C-terminal NADH-binding domain forming a Rossmann fold, and a three beta-stranded linker region connecting these two domains. The FAD cofactor is located in the cleft between the two domains and interacts primarily with the FAD-binding domain	Ulva prolifera

Organism

Organism	UniProt	Comment	Textmining
Ulva prolifera	A0A286R227	cf. EC 1.7.1.1	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2 ferricyanide + NADH + H+	-	Ulva prolifera	2 ferrocyanide + NAD+	-	?

Cofactor

Cofactor	Comment	Organism	Structure
FAD	the FAD cofactor is located in the cleft between the N-terminal FAD-binding domain and the C-terminal NADH-binding domain. The cofactor is located in the cleft between the two domains and interacts primarily with the FAD-binding domain	Ulva prolifera

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Release 2023.1 (January 2023)