Structure-based studies on the metal binding of two-metal-dependent sugar isomerases - Wikidata - thesis-toulmin - TriplyDB

Structure-based studies on the metal binding of two-metal-dependent sugar isomerases

Structure-based studies on the metal binding of two-metal-dependent sugar isomerases

http://www.wikidata.org/entity/Q27690726

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Characterization of a Mannose-6-Phosphate Isomerase from Bacillus amyloliquefaciens and Its Application in Fructose-6-Phosphate Production A highly efficient sorbitol dehydrogenase from Gluconobacter oxydans G624 and improvement of its stability through immobilization Isomerases for biotransformation of D-hexoses.Bioproduction of D-Tagatose from D-Galactose Using Phosphoglucose Isomerase from Pseudomonas aeruginosa PAO1.

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Structure-based studies on the metal binding of two-metal-dependent sugar isomerases

http://www.wikidata.org/entity/Q27690726

description

2014 nî lūn-bûn

@nan

2014 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Structure-based studies on the metal binding of two-metal-dependent sugar isomerases

@ast

Structure-based studies on the metal binding of two-metal-dependent sugar isomerases

@en

Structure-based studies on the metal binding of two-metal-dependent sugar isomerases

@nl

type

label

Structure-based studies on the metal binding of two-metal-dependent sugar isomerases

@ast

Structure-based studies on the metal binding of two-metal-dependent sugar isomerases

@en

Structure-based studies on the metal binding of two-metal-dependent sugar isomerases

@nl

prefLabel

Structure-based studies on the metal binding of two-metal-dependent sugar isomerases

@ast

Structure-based studies on the metal binding of two-metal-dependent sugar isomerases

@en

Structure-based studies on the metal binding of two-metal-dependent sugar isomerases

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Structure-based studies on the metal binding of two-metal-dependent sugar isomerases

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Jung-Kul Lee

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Lin-Woo Kang

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Myoung-Ki Hong

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Ponnandy Prabhu

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Raushan Singh

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Sun Chang Kim

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Thi-Ngoc-Thanh Doan

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P2860

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

The structure of rhamnose isomerase from Escherichia coli and its relation with xylose isomerase illustrates a change between inter and intra-subunit complementation during evolution

Structural insight into Ca2+ specificity in tetrameric cation channels

Zinc Coordination Geometry and Ligand Binding Affinity: The Structural and Kinetic Analysis of the Second-Shell Serine 228 Residue and the Methionine 180 Residue of the Aminopeptidase from Vibrio proteolyticus †

A metal-mediated hydride shift mechanism for xylose isomerase based on the 1.6 A Streptomyces rubiginosus structures with xylitol and D-xylose

Catalytic reaction mechanism of Pseudomonas stutzeri L-rhamnose isomerase deduced from X-ray structures

Metal Ion Roles and the Movement of Hydrogen during Reaction Catalyzed by D-Xylose Isomerase: A Joint X-Ray and Neutron Diffraction Study

Evidence of the Participation of Remote Residues in the Catalytic Activity of Co-Type Nitrile Hydratase from Pseudomonas putida

Identification of the elusive hydronium ion exchanging roles with a proton in an enzyme at lower pH values

Mechanism for aldose-ketose interconversion by D-xylose isomerase involving ring opening followed by a 1,2-hydride shift

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3446-59

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scholarly article

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3490427

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10.1111/FEBS.12872

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15

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281

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Manish Kumar Tiwari

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2014-08-01T00:00:00Z

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263100888

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24925069

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