Enhancing H2O2 resistance of an esterase from Pyrobaculum calidifontis by structure-guided engineering of the substrate binding site. (Q50201658)

27 February 2018

title

Enhancing H2O2 resistance of an esterase from Pyrobaculum calidifontis by structure-guided engineering of the substrate binding site. (English)

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27 February 2018

author name string

Pengfei Zhou

1

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27 February 2018

Dongming Lan

2

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27 February 2018

Grzegorz Maria Popowicz

3

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27 February 2018

Xuping Wang

4

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27 February 2018

Bo Yang

5

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27 February 2018

Yonghua Wang

6

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27 February 2018

language of work or name

English

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publication date

17 May 2017

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27 February 2018

Applied Microbiology and Biotechnology

published in

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27 February 2018

volume

101

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issue

14

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27 February 2018

page(s)

5689-5697

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27 February 2018

https://scigraph.springernature.com/pub.10.1007/s00253-017-8299-0

exact match

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21 January 2018

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Enhancement of hydrogen peroxide stability of a novel Anabaena sp. DyP-type peroxidase by site-directed mutagenesis of methionine residues.

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The crystal structure of an esterase from the hyperthermophilic microorganism Pyrobaculum calidifontis VA1 explains its enantioselectivity

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10.1007/S00253-017-8299-0

21 January 2018

Identifiers

DOI

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27 February 2018

PubMed ID

28516207

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27 February 2018