Redesigning secondary structure to invert coenzyme specificity in isopropylmalate dehydrogenase. - Wikidata - awgldk - TriplyDB

Redesigning secondary structure to invert coenzyme specificity in isopropylmalate dehydrogenase.

Redesigning secondary structure to invert coenzyme specificity in isopropylmalate dehydrogenase.

http://www.wikidata.org/entity/Q30425730

about

Computational design of Candida boidinii xylose reductase for altered cofactor specificity Probing the determinants of coenzyme specificity in ferredoxin-NADP+ reductase by site-directed mutagenesis Engineering Nucleotide Specificity of Succinyl-CoA Synthetase in Blastocystis: The Emerging Role of Gatekeeper Residues Structural plasticity of an aminoacyl-tRNA synthetase active site A novel serine hydroxymethyltransferase from Arthrobacter nicotianae: characterization and improving catalytic efficiency by rational design.Molecular determinants of the cofactor specificity of ribitol dehydrogenase, a short-chain dehydrogenase/reductase Protein engineering reveals ancient adaptive replacements in isocitrate dehydrogenase.Functional prediction: identification of protein orthologs and paralogs Quantitative chimeric analysis of six specificity determinants that differentiate Escherichia coli aspartate from tyrosine aminotransferase.Structure-guided alteration of coenzyme specificity of formate dehydrogenase by saturation mutagenesis to enable efficient utilization of NADP+.A receptor dependent-4D QSAR approach to predict the activity of mutated enzymes.Changing the target base specificity of the EcoRV DNA methyltransferase by rational de novo protein-design.Switch in Cofactor Specificity of a Baeyer-Villiger Monooxygenase.Localization and nucleotide specificity of Blastocystis succinyl-CoA synthetase.Site-saturation mutagenesis is more efficient than DNA shuffling for the directed evolution of beta-fucosidase from beta-galactosidase.Structure-based conversion of the coenzyme requirement of a short-chain dehydrogenase/reductase involved in bacterial alginate metabolism.The coenzyme specificity of Candida tenuis xylose reductase (AKR2B5) explored by site-directed mutagenesis and X-ray crystallography.Engineering of coenzyme specificity of formate dehydrogenase from Saccharomyces cerevisiae Crystal structures of mutants of Thermus thermophilus IPMDH adapted to low temperatures.Characterization of homoisocitrate dehydrogenase involved in lysine biosynthesis of an extremely thermophilic bacterium, Thermus thermophilus HB27, and evolutionary implication of beta-decarboxylating dehydrogenase.Comparison of isocitrate dehydrogenase from three hyperthermophiles reveals differences in thermostability, cofactor specificity, oligomeric state, and phylogenetic affiliation.Complete reversal of coenzyme specificity of xylitol dehydrogenase and increase of thermostability by the introduction of structural zinc.A genetically encoded tool for manipulation of NADP+/NADPH in living cells.Protein Engineering for Nicotinamide Coenzyme Specificity in Oxidoreductases: Attempts and Challenges.A computational strategy for altering an enzyme in its cofactor preference to NAD(H) and/or NADP(H).

P2860

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P2860

Redesigning secondary structure to invert coenzyme specificity in isopropylmalate dehydrogenase.

http://www.wikidata.org/entity/Q30425730

description

1996 nî lūn-bûn

@nan

1996 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1996 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

1996年の論文

@ja

1996年論文

@yue

1996年論文

@zh-hant

1996年論文

@zh-hk

1996年論文

@zh-mo

1996年論文

@zh-tw

1996年论文

@wuu

name

Redesigning secondary structur ...... isopropylmalate dehydrogenase.

@en

type

label

Redesigning secondary structur ...... isopropylmalate dehydrogenase.

@en

prefLabel

Redesigning secondary structur ...... isopropylmalate dehydrogenase.

@en

P1433

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P2860

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P356

PNAS.93.22.12171

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Redesigning secondary structur ...... isopropylmalate dehydrogenase.

@en

P2093

A Greer

http://www.w3.org/2001/XMLSchema#string

A M Dean

http://www.w3.org/2001/XMLSchema#string

R Chen

http://www.w3.org/2001/XMLSchema#string

P2860

DNA sequencing with chain-terminating inhibitors

Characterization of a cDNA clone for human NAD(+)-specific isocitrate dehydrogenase alpha-subunit and structural comparison with its isoenzymes from different species

Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase

Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 A resolution

Catalytic mechanism of NADP(+)-dependent isocitrate dehydrogenase: implications from the structures of magnesium-isocitrate and NADP+ complexes

Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase

Structure of 3-isopropylmalate dehydrogenase in complex with NAD+: ligand-induced loop closing and mechanism for cofactor specificity

Rapid and efficient site-specific mutagenesis without phenotypic selection

Chemical and biological evolution of nucleotide-binding protein

Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension

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12171-12176

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scholarly article

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10.1073/PNAS.93.22.12171

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22

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