Entropic and enthalpic components of catalysis in the mutase and lyase activities of Pseudomonas aeruginosa PchB. (Q35184901)

7 August 2017

title

Entropic and enthalpic components of catalysis in the mutase and lyase activities of Pseudomonas aeruginosa PchB. (English)

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7 August 2017

main subject

Pseudomonas aeruginosa

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author name string

Qianyi Luo

series ordinal

1

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7 August 2017

Kathleen M Meneely

series ordinal

2

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7 August 2017

Audrey L Lamb

series ordinal

3

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7 August 2017

language of work or name

English

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publication date

19 April 2011

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Journal of the American Chemical Society

7 August 2017

published in

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7 August 2017

volume

133

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7 August 2017

issue

18

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7 August 2017

page(s)

7229-7233

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BLAST+: architecture and applications

7 August 2017

cites work

1 reference

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The crystal structure of chorismate lyase shows a new fold and a tightly retained product

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Structure-function analyses of isochorismate-pyruvate lyase from Pseudomonas aeruginosa suggest differing catalytic mechanisms for the two pericyclic reactions of this bifunctional enzyme

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27 September 2018

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12 December 2020

Small scale biosynthesis and purification of gram quantities of chorismic acid

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12 December 2020

Mechanisms related to enzyme catalysis

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12 December 2020

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12 December 2020

Identifiers

DOI

10.1021/JA202091A

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7 August 2017

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7 August 2017

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