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Literature summary for 1.5.1.40 extracted from

  • Warkentin, E.; Mamat, B.; Sordel-Klippert, M.; Wicke, M.; Thauer, R.K.; Iwata, M.; Iwata, S.; Ermler, U.; Shima, S.
    Structures of F420H2:NADP+ oxidoreductase with and without its substrates bound (2001), EMBO J., 20, 6561-6569.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Archaeoglobus fulgidus

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapour diffusion method, crystal structure of the enzyme bound with coenzyme F420. The structure resolved to 1.65 A contains two domains: an N-terminal domain characteristic of a dinucleotide-binding Rossmann fold and a smaller C-terminal domain. The nicotinamide and the deazaflavin part of the two coenzymes are bound in the cleft between the domains such that the Si-faces of both face each other at a distance of 3.1 A, which is optimal for hydride transfer Archaeoglobus fulgidus

Organism

Organism UniProt Comment Textmining
Archaeoglobus fulgidus O29370
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
reduced coenzyme F420 + NADP+ of the two substrates NADP+ has to bind first, the binding being associated with an induced fit. The stereochemical analysis of the hydrode transfer leads to the conclusion that the observed orientation of the Si-face of coenzyme F420 towards the Si-face of NADP+ allows only the transfer of the proS hydrogen at C5 to the proS position at C4 and vice versa Archaeoglobus fulgidus oxidized coenzyme F420 + NADPH + H+
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Synonyms

Synonyms Comment Organism
AF0892
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Archaeoglobus fulgidus
F420H2:NADP+ oxidoreductase
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Archaeoglobus fulgidus
Fno
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Archaeoglobus fulgidus