Essential role of the metal-ion in the IPM-assisted domain closure of 3-isopropylmalate dehydrogenase.

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Glutamate 270 plays an essential role in K(+)-activation and domain closure of Thermus thermophilus isopropylmalate dehydrogenase

P2860

Q27696836-B64335D3-9320-4556-9F61-9F53F87D7422

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Essential role of the metal-ion in the IPM-assisted domain closure of 3-isopropylmalate dehydrogenase.

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http://www.wikidata.org/entity/Q54352469

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2011 nî lūn-bûn

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2011年の論文

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2011年学术文章

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2011年学术文章

@zh-cn

2011年学术文章

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2011年学术文章

@zh-my

2011年学术文章

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2011年學術文章

@yue

2011年學術文章

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2011年學術文章

@zh-hant

name

Essential role of the metal-io ...... isopropylmalate dehydrogenase.

@en

Essential role of the metal-io ...... isopropylmalate dehydrogenase.

@nl

type

Item

label

Essential role of the metal-io ...... isopropylmalate dehydrogenase.

@en

Essential role of the metal-io ...... isopropylmalate dehydrogenase.

@nl

prefLabel

Essential role of the metal-io ...... isopropylmalate dehydrogenase.

@en

Essential role of the metal-io ...... isopropylmalate dehydrogenase.

@nl

P1476

Essential role of the metal-io ...... isopropylmalate dehydrogenase.

@en

P2093

Adrienn Bodonyi

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

András Bacsó

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

Eva Gráczer

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

Mária Vas

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

Peter V Konarev

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

Péter Závodszky

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

Tamás Szimler

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

P2860

Atomic level description of the domain closure in a dimeric enzyme: thermus thermophilus 3-isopropylmalate dehydrogenase

Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus

A hierarchy of timescales in protein dynamics is linked to enzyme catalysis

CRYSOL– a Program to Evaluate X-ray Solution Scattering of Biological Macromolecules from Atomic Coordinates

Exploring the range of protein flexibility, from a structural proteomics perspective.

The role of glutamate 87 in the kinetic mechanism of Thermus thermophilus isopropylmalate dehydrogenase.

Insight into the mechanism of domain movements and their role in enzyme function: example of 3-phosphoglycerate kinase.

Ellman's reagent: 5,5'-dithiobis(2-nitrobenzoic acid)--a reexamination.

Long-range nonradiative transfer of electronic excitation energy in proteins and polypeptides.

Rates of unfolding, rather than refolding, determine thermal stabilities of thermophilic, mesophilic, and psychrotrophic 3-isopropylmalate dehydrogenases.

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3297-3302

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scholarly article

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10.1016/J.FEBSLET.2011.09.013

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

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English

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

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585

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

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Dmitri Svergun

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2011-09-17T00:00:00Z

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

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51663178

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

P698

21939659

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

Essential role of the metal-ion in the IPM-assisted domain closure of 3-isopropylmalate dehydrogenase.

about

P2860

P2860

Essential role of the metal-ion in the IPM-assisted domain closure of 3-isopropylmalate dehydrogenase.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698