Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase binary and ternary complexes. Specificity and catalytic mechanism

Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase binary and ternary complexes. Specificity and catalytic mechanism

Item
http://www.wikidata.org/entity/Q27639527
Medium- and short-chain dehydrogenase/reductase gene and protein families : the SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymesCharacterization of mannitol-2-dehydrogenase in Saccharina japonica: evidence for a new polyol-specific long-chain dehydrogenases/reductaseDynamic mechanism of proton transfer in mannitol 2-dehydrogenase from Pseudomonas fluorescens: mobile GLU292 controls proton relay through a water channel that connects the active site with bulk solvent.Detecting coevolution in and among protein domainsBiosynthesis of aminocyclitol-aminoglycoside antibiotics and related compounds.A highly efficient sorbitol dehydrogenase from Gluconobacter oxydans G624 and improvement of its stability through immobilizationCrystallization, preliminary X-ray diffraction and structure analysis of Thermotoga maritima mannitol dehydrogenase.The coenzyme specificity of Candida tenuis xylose reductase (AKR2B5) explored by site-directed mutagenesis and X-ray crystallography.Quantitative functional characterization of conserved molecular interactions in the active site of mannitol 2-dehydrogenase.From alcohol dehydrogenase to a "one-way" carbonyl reductase by active-site redesign: a mechanistic study of mannitol 2-dehydrogenase from pseudomonas fluorescens.On the role of Brønsted catalysis in Pseudomonas fluorescens mannitol 2-dehydrogenase.Frequencies of hydrophobic and hydrophilic runs and alternations in proteins of known structure.Molecular dynamics simulation studies of the wild-type, I21V, and I16T mutants of isoniazid-resistant Mycobacterium tuberculosis enoyl reductase (InhA) in complex with NADH: toward the understanding of NADH-InhA different affinities.The oxyanion hole of Pseudomonas fluorescens mannitol 2-dehydrogenase: a novel structural motif for electrostatic stabilization in alcohol dehydrogenase active sites.Structure-guided engineering of the coenzyme specificity of Pseudomonas fluorescens mannitol 2-dehydrogenase to enable efficient utilization of NAD(H) and NADP(H).Role of mannitol dehydrogenases in osmoprotection of Gluconobacter oxydans.
P2860

Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase binary and ternary complexes. Specificity and catalytic mechanism

Item
http://www.wikidata.org/entity/Q27639527
description
2002 nî lūn-bûn
@nan
2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի նոյեմբերին հրատարակված գիտական հոդված
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2002年の論文
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2002年学术文章
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2002年学术文章
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2002年学术文章
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2002年学术文章
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2002年学术文章
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2002年學術文章
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name
Crystal structure of Pseudomon ...... ficity and catalytic mechanism
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Crystal structure of Pseudomon ...... ficity and catalytic mechanism
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Crystal structure of Pseudomon ...... ficity and catalytic mechanism
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type
label
Crystal structure of Pseudomon ...... ficity and catalytic mechanism
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Crystal structure of Pseudomon ...... ficity and catalytic mechanism
@en
Crystal structure of Pseudomon ...... ficity and catalytic mechanism
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prefLabel
Crystal structure of Pseudomon ...... ficity and catalytic mechanism
@ast
Crystal structure of Pseudomon ...... ficity and catalytic mechanism
@en
Crystal structure of Pseudomon ...... ficity and catalytic mechanism
@nl
P1433
P1476
P2093
P2860
P304
P31
P3181
P356
P407
P433
P478
P50
P577
P698
P921
P3181
P356
P1433
P1476
Crystal structure of Pseudomon ...... ficity and catalytic mechanism
@en
P2093
P2860
P304
P31
P3181
P356
P407
P433
P478
P50
P577
P698
P921