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Literature summary extracted from

  • Klimacek, M.; Nidetzky, B.
    A catalytic consensus motif for D-mannitol 2-dehydrogenase, a member of a polyol-specific long-chain dehydrogenase family, revealed by kinetic characterization of site-directed mutants of the enzyme from Pseudomonas fluorescens (2002), Biochem. J., 367, 13-18.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.67 expression of wild-type enzyme and mutant enzymes in Escherichia coli Pseudomonas fluorescens

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.67 H303A mutant enzyme displays catalytic efficiency for NAD+-dependent oxidation of D-mannitol 300fold below the wild-type value Pseudomonas fluorescens
1.1.1.67 K295A mutant enzyme displays catalytic efficiency for NAD+-dependent oxidation of D-mannitol 400000fold below the wild-type value Pseudomonas fluorescens
1.1.1.67 N300A mutant enzyme displays catalytic efficiency for NAD+-dependent oxidation of D-mannitol 1000fold below the wild-type value Pseudomonas fluorescens

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.67 Pseudomonas fluorescens
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.67 D-fructose + NADH + H+ Asn300 has an auxiliary role in stabilization of the transition state of hydride transfer and His303 contributes to substrate positioning, role of Lys295 in general base enzymic catalysis Pseudomonas fluorescens D-mannitol + NAD+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.67 M2DH
-
 Pseudomonas fluorescens
1.1.1.67 PsM2DH
-
 Pseudomonas fluorescens