less stable enzyme, dulcitol-inducible, accounts for oxidation of certain fully hydroxylated polyols containing a D-threo-configuration adjacent to a primary alcohol
less stable enzyme, dulcitol-inducible, accounts for oxidation of certain fully hydroxylated polyols containing a D-threo-configuration adjacent to a primary alcohol
the enzyme BjSDH is part of the superfamily of Zn-independent short-chain dehydrogenases. The BjSDH structure folds in the Rossmann fold, which is typical for NADH-dependent enzymes and the SDR family
the enzyme BjSDH is part of the superfamily of Zn-independent short-chain dehydrogenases. The BjSDH structure folds in the Rossmann fold, which is typical for NADH-dependent enzymes and the SDR family
a continuous beta-sheet is formed between two monomers in the tetramer. The BjSDH structure folds in the Rossmann fold. The monomer of BjSDH is composed of a central parallel beta-sheet surrounded by three alpha-helices on each side. At the top of the beta-sheet a small helix–turn–helix motif is located between the two final beta-strands betaF and betaG. Tetrameric quaternary organization, structure comparisons, overview
a continuous beta-sheet is formed between two monomers in the tetramer. The BjSDH structure folds in the Rossmann fold. The monomer of BjSDH is composed of a central parallel beta-sheet surrounded by three alpha-helices on each side. At the top of the beta-sheet a small helix–turn–helix motif is located between the two final beta-strands betaF and betaG. Tetrameric quaternary organization, structure comparisons, overview
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UNIPROT
LITERATURE
purified recombinant His-tagged enzyme in complex with both NAD+ and glucitol, X-ray diffraction structure determination and analysis at 2.9 A resolution, molecular replacement and modelling
gene SDh, DNA and amino acid sequence determination and analysis, isolation, characterization and evaluation of the Pichia pastoris sorbitol dehydrogenase promoter for expression of heterologous proteins, recombinant expression of several different enzymes using the SDH promoter, overview
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1.1.1.15 D-iditol 2-dehydrogenase
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