The three-dimensional structure of AKR11B4, a glycerol dehydrogenase from Gluconobacter oxydans, reveals a tryptophan residue as an accelerator of reaction turnover. [electronic resource]
Producer: 20101216Description: 353-62 p. digitalISSN:- 1089-8638
- Amino Acid Sequence
- Amino Acid Substitution
- Apraxia, Ideomotor
- Bacterial Proteins -- chemistry
- Catalytic Domain -- genetics
- Crystallography, X-Ray
- Gluconobacter oxydans -- enzymology
- Hydrophobic and Hydrophilic Interactions
- Models, Molecular
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- NADP -- metabolism
- Protein Conformation
- Recombinant Proteins -- chemistry
- Sequence Homology, Amino Acid
- Static Electricity
- Structural Homology, Protein
- Substrate Specificity
- Sugar Alcohol Dehydrogenases -- chemistry
- Tryptophan -- chemistry
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Publication Type: Journal Article
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