(Q27758273)

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25 December 2024

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Y. F. Li

1

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25 December 2024

Y. Hata

2

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25 December 2024

T. Fujii

3

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25 December 2024

T. Hisano

4

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M. Nishihara

5

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25 December 2024

T. Kurihara

6

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N. Esaki

7

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full work available at URL

25 December 2024

language of work or name

English

0 references

publication date

12 June 1998

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http://www.jbc.org/article/S0021925819653871/pdf

1 reference

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https://api.elsevier.com/content/article/PII:S0021925819653871?httpAccept=text/xml

25 December 2024

1 reference

https://api.crossref.org/works/10.1074/JBC.273.24.15035

https://api.elsevier.com/content/article/PII:S0021925819653871?httpAccept=text/plain

25 December 2024

1 reference

https://api.crossref.org/works/10.1074/JBC.273.24.15035

https://syndication.highwire.org/content/doi/10.1074/jbc.273.24.15035

25 December 2024

1 reference

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Journal of Biological Chemistry

25 December 2024

published in

0 references

volume

273

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issue

24

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page(s)

15035-44

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cites work

Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.24.15035

The alpha/beta hydrolase fold

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.24.15035

Comprehensive site-directed mutagenesis of L-2-halo acid dehalogenase to probe catalytic amino acid residues.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.24.15035

Refined X-ray structures of haloalkane dehalogenase at pH 6.2 and pH 8.2 and implications for the reaction mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.24.15035

Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.24.15035

Structure of 4-chlorobenzoyl coenzyme A dehalogenase determined to 1.8 A resolution: an enzyme catalyst generated via adaptive mutation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.24.15035

Rapid and efficient site-specific mutagenesis without phenotypic selection

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.24.15035

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.24.15035

The CCP4 suite: programs for protein crystallography

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.24.15035

Crystallization and preliminary x-ray crystallographic studies of L-2-haloacid dehalogenase from Pseudomonas sp. YL

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.24.15035

Paracatalytic inactivation of L-2-haloacid dehalogenase from Pseudomonas sp. YL by hydroxylamine. Evidence for the formation of an ester intermediate

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.24.15035

Evidence for nucleophilic catalysis in the aromatic substitution reaction catalyzed by (4-chlorobenzoyl)coenzyme A dehalogenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.24.15035

2-Haloacid dehalogenase from a 4-chlorobenzoate-degrading Pseudomonas spec. CBS 3.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.24.15035

Reconsideration of the essential role of a histidine residue of L-2-halo acid dehalogenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.24.15035

Characterization of the haloacid dehalogenase from Xanthobacter autotrophicus GJ10 and sequencing of the dhlB gene

21 January 2018

8

1 reference

https://api.crossref.org/works/10.1074/JBC.273.24.15035

Purification and characterization of thermostable and nonthermostable 2-haloacid dehalogenases with different stereospecificities from Pseudomonas sp. strain YL

25 December 2024

17

1 reference

https://api.crossref.org/works/10.1074/JBC.273.24.15035

Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO

25 December 2024

21

1 reference

https://api.crossref.org/works/10.1074/JBC.273.24.15035