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Literature summary for 1.1.1.25 extracted from

  • Vogan, E.
    Shikimate dehydrogenase structure reveals novel fold (2003), Structure, 11, 902-903.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Methanocaldococcus jannaschii fourth enzyme in the shikimate biosynthetic pathway ?
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?

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information fourth enzyme in the shikimate biosynthetic pathway Methanocaldococcus jannaschii ?
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?

Subunits

Subunits Comment Organism
More the structure reveals an enzyme with a deep cleft, which contains the active site, formed at the junction of two domains. The C-terminal domain is easily recognizable as a Rossmann fold dinucleotide binding domain, responsible for binding the NADP cofactor. The N-terminal substrate binding and dimerization domain, an alpha-beta-alpha sandwich, represents a unique topological fold, structure modeling Methanocaldococcus jannaschii

Synonyms

Synonyms Comment Organism
SDH
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Methanocaldococcus jannaschii
shikimate 5-dehydrogenase
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Methanocaldococcus jannaschii

Cofactor

Cofactor Comment Organism Structure
additional information dinucleotide cofactor binding domain structure is a Rossmann fold Methanocaldococcus jannaschii