Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase - Wikidata - awgldk - TriplyDB

Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase

Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase

http://www.wikidata.org/entity/Q24675416

about

Role of the divalent metal ion in the NAD:malic enzyme reaction: an ESEEM determination of the ground state conformation of malate in the E:Mn:malate complex.Molecular and phylogenetic characterization of isopropylmalate dehydrogenase of a thermoacidophilic archaeon, Sulfolobus sp. strain 7.Crystal structures of mutants of Thermus thermophilus IPMDH adapted to low temperatures.Comparison of isocitrate dehydrogenase from three hyperthermophiles reveals differences in thermostability, cofactor specificity, oligomeric state, and phylogenetic affiliation.Novel substrate specificity of designer 3-isopropylmalate dehydrogenase derived from Thermus thermophilus HB8.Cold-adaptation mechanism of mutant enzymes of 3-isopropylmalate dehydrogenase from Thermus thermophilus.

P2860

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P2860

Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase

http://www.wikidata.org/entity/Q24675416

description

1995 nî lūn-bûn

@nan

1995 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

1995 թվականի հունվարին հրատարակված գիտական հոդված

@hy

1995年の論文

@ja

1995年論文

@yue

1995年論文

@zh-hant

1995年論文

@zh-hk

1995年論文

@zh-mo

1995年論文

@zh-tw

1995年论文

@wuu

name

Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase

@ast

Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase

@en

Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase

@nl

type

label

Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase

@ast

Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase

@en

Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase

@nl

prefLabel

Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase

@ast

Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase

@en

Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase

@nl

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P2860

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Protein Science

P1476

Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase

@en

P2093

D E Koshland

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

T Zhang

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

P2860

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

A general method applicable to the search for similarities in the amino acid sequence of two proteins

The role and control of the glyoxylate cycle in Escherichia coli

Automated docking of substrates to proteins by simulated annealing.

Molecular cloning of the isocitrate dehydrogenase gene of an extreme thermophile, Thermus thermophilus HB8

Histidine in the nucleotide-binding site of NADP-linked isocitrate dehydrogenase from pig heart.

Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5-A resolution: a pseudo-Michaelis ternary complex.

Electrostatic and steric contributions to regulation at the active site of isocitrate dehydrogenase.

Use of intermediate partitioning to calculate intrinsic isotope effects for the reaction catalyzed by malic enzyme.

P304

84-92

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

P31

scholarly article

P356

10.1002/PRO.5560040111

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

P407

P433

1

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P478

4

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1995-01-01T00:00:00Z

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15426375

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7773180

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2142962

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