(Q41859069)

English

An amino acid at position 142 in nitrilase from Rhodococcus rhodochrous ATCC 33278 determines the substrate specificity for aliphatic and aromatic nitriles

scientific article published on November 2008

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

An amino acid at position 142 in nitrilase from Rhodococcus rhodochrous ATCC 33278 determines the substrate specificity for aliphatic and aromatic nitriles (English)

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

Rhodococcus rhodochrous

object named as

Rhodococcus rhodochrous

1 reference

based on heuristic

inferred from title

author name string

Soo-Jin Yeom

1

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

Hye-Jung Kim

2

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

Jung-Kul Lee

3

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

Dong-Eun Kim

4

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

Deok-Kun Oh

5

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

language of work or name

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publication date

1 November 2008

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Europe PubMed Central

PMC publication ID

13 October 2017

Biochemical Journal

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Europe PubMed Central

PMC publication ID

13 October 2017

415

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Europe PubMed Central

PMC publication ID

13 October 2017

3

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

401-407

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

copyright license

Creative Commons Attribution-NonCommercial 2.5 Generic

25 July 2019

1 reference

April 2022 Public Data File from Crossref

copyright status

0 references

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1 reference

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The nitrilase family of CN hydrolysing enzymes - a comparative study

1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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Nitrilase of Rhodococcus rhodochrous J1. Purification and characterization

1 reference

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Mechanistic and structural studies on Rhodococcus ATCC 39484 nitrilase

1 reference

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

1 reference

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Influence of different carboxy-terminal mutations on the substrate-, reaction- and enantiospecificity of the arylacetonitrilase from Pseudomonas fluorescens EBC191.

1 reference

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Post-translational cleavage of recombinantly expressed nitrilase from Rhodococcus rhodochrous J1 yields a stable, active helical form.

1 reference

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1 reference

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Detection of covalent enzyme-substrate complexes of nitrilase by ion-spray mass spectroscopy

1 reference

https://pubmed.ncbi.nlm.nih.gov/18412544

12 December 2020

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inferred from PubMed ID database lookup

Identifiers

10.1042/BJ20080440

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 October 2017

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