Literature summary for 1.12.99.6 extracted from

Dias, A.V.; Mulvihill, C.M.; Leach, M.R.; Pickering, I.J.; George, G.N.; Zamble, D.B.
Structural and biological analysis of the metal sites of Escherichia coli hydrogenase accessory protein HypB (2008), Biochemistry, 47, 11981-11991.

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Activating Compound

Activating Compound	Comment	Organism	Structure
HypB	accessory protein HypB is necessary for the production of active hydrogenase	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ni2+	accessory protein HypB is necessary for Ni(II) incorporation into the hydrogenase protein. HypB has two metal-binding sites, a high-affinity Ni(II) site that includes ligands from the N-terminal domain and a low-affinity metal site located within the C-terminal GTPase domain	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
H2 + oxidized benzyl viologen	-	Escherichia coli	H+ + reduced benzyl viologen	-	?

Synonyms

Synonyms	Comment	Organism
[NiFe]-hydrogenase	-	Escherichia coli

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Release 2023.1 (January 2023)