Literature summary for 1.3.99.B12 extracted from

Hemmi, H.; Takahashi, Y.; Shibuya, K.; Nakayama, T.; Nishino, T.
Menaquinone-specific prenyl reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus (2005), J. Bacteriol., 187, 1937-1944.

Search for more literature for 1.3.99.B12

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Archaeoglobus fulgidus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
menaquinone-7 + reduced acceptor	Archaeoglobus fulgidus	the enzyme is involved in the biosynthesis of menaquinone-7(14H) i.e. menaquinone with a fully saturated heptaprenyl side chain	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Archaeoglobus fulgidus	O29609	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Archaeoglobus fulgidus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
menaquinone-7 + reduced acceptor	the enzyme is involved in the biosynthesis of menaquinone-7(14H) i.e. menaquinone with a fully saturated heptaprenyl side chain	Archaeoglobus fulgidus	?	-	?
menaquinone-7 + reduced dithionite	menaquinone-7 i.e. menaquinone with a fully saturated heptaprenyl side chain. The enzyme specifically reduces the prenyl side chain of menaquinone, whereas the prenyl moieties of ubiquinone-8 and geranygeranyl diphosphates are relatively resistant to reduction. The enzyme is not able to utilize NAD(P)H as the electron donor	Archaeoglobus fulgidus	menaquinone-7 with partially saturated prenyl side chain + dithionite	-	?

Synonyms

Synonyms	Comment	Organism
AF0648	-	Archaeoglobus fulgidus
menaquinone-specific prenyl reductase	misleading	Archaeoglobus fulgidus

Cofactor

Cofactor	Comment	Organism	Structure
FAD	noncovalently bound to the enzyme	Archaeoglobus fulgidus

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Release 2023.1 (January 2023)