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Literature summary for 1.1.1.138 extracted from

  • Klimacek, M.; Kavanagh, K.L.; Wilson, D.K.; Nidetzky, B.
    Pseudomonas fluorescens mannitol 2-dehydrogenase and the family of polyol-specific long-chain dehydrogenases/reductases: sequence-based classification and analysis of structure-function relationships (2003), Chem. Biol. Interact., 143-144, 559-582.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no metal cofactor required Pseudomonas fluorescens

Organism

Organism UniProt Comment Textmining
Pseudomonas fluorescens
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information specific for transferring the 4-pro-S hydrogen from NAD(P)H Pseudomonas fluorescens ?
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?

Subunits

Subunits Comment Organism
More structure-function analysis of enzyme and the family of polyol-specific long-chain dehydrogenases/reductases. G33 is in the N-terminal coenzyme-binding domain, D230 and K295 are at an interdomain segment contributing to the active site in which K295 likely functions as the catalytic general acid/base Pseudomonas fluorescens

Synonyms

Synonyms Comment Organism
PSLDR
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Pseudomonas fluorescens