Cold-adaptation mechanism of mutant enzymes of 3-isopropylmalate dehydrogenase from Thermus thermophilus (Q44040013)

29 November 2017

Cold-adaptation mechanism of mutant enzymes of 3-isopropylmalate dehydrogenase from Thermus thermophilus (English)

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29 November 2017

Thermus thermophilus

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Toshiharu Suzuki

1

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29 November 2017

Masako Yasugi

2

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29 November 2017

Fumio Arisaka

3

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29 November 2017

Tairo Oshima

4

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29 November 2017

Akihiko Yamagishi

5

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29 November 2017

language of work or name

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1 June 2002

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Protein Engineering Design and Selection

29 November 2017

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29 November 2017

15

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29 November 2017

6

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29 November 2017

471-476

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Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

29 November 2017

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https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

Effects of point mutations in a hinge region on the stability, folding, and enzymatic activity of Escherichia coli dihydrofolate reductase

21 January 2018

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https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme

21 January 2018

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https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

Electrostatic effects play a central role in cold adaptation of trypsin

21 January 2018

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https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

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

21 January 2018

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https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

Substrate-induced conformational change in a trimeric ornithine transcarbamoylase

21 January 2018

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https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

The C9 methyl group of retinal interacts with glycine-121 in rhodopsin.

21 January 2018

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https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

A stable intermediate in the thermal unfolding process of a chimeric 3-isopropylmalate dehydrogenase between a thermophilic and a mesophilic enzymes

21 January 2018

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https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

Crystal structures of mutants of Thermus thermophilus IPMDH adapted to low temperatures

21 January 2018

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https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

Structure of 3-isopropylmalate dehydrogenase in complex with 3-isopropylmalate at 2.0 A resolution: the role of Glu88 in the unique substrate-recognition mechanism

21 January 2018

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https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

Thermodynamic activation parameters of fish myofibrillar ATPase enzyme and evolutionary adaptations to temperature

21 January 2018

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https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

Ligand-induced changes in the conformation of 3-isopropylmalate dehydrogenase from Thermus thermophilus

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

21 January 2018

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https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

Rapid and efficient site-specific mutagenesis without phenotypic selection

21 January 2018

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https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility

21 January 2018

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https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

A mutation at the interface between domains causes rearrangement of domains in 3-isopropylmalate dehydrogenase

21 January 2018

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https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

21 January 2018

Cold adapted enzymes.

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https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

Adaptation of a thermophilic enzyme, 3-isopropylmalate dehydrogenase, to low temperatures

21 January 2018

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https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

Screening of stable proteins in an extreme thermophile, Thermus thermophilus.

21 January 2018

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https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

Crystal structure of 3-isopropylmalate dehydrogenase from the moderate facultative thermophile, Bacillus coagulans: two strategies for thermostabilization of protein structures

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

The effects of heme pocket hydrophobicity on the ligand binding dynamics in myoglobin as studied with leucine 29 mutants

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

Cold adaptation of the thermophilic enzyme 3-isopropylmalate dehydrogenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase

21 January 2018

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https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

Structural invariants in protein folding

21 January 2018

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https://api.crossref.org/works/10.1093%2FPROTEIN%2F15.6.471

21 January 2018

Identifiers

DOI

10.1093/PROTEIN/15.6.471

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29 November 2017

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