Engineering enzyme access tunnels

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00159816%3A_____%2F19%3A00072464" target="_blank" >RIV/00159816:_____/19:00072464 - isvavai.cz</a>

Alternative codes found

RIV/00216224:14310/19:00113351

Result on the web

<a href="https://reader.elsevier.com/reader/sd/pii/S0734975019300679?token=07A73AF725622471204758E7172B19D66B5AB1943E6199EC3408B4A96DCC22ED6EDA0697937AF5F98AF1FDC25F8347BF" target="_blank" >https://reader.elsevier.com/reader/sd/pii/S0734975019300679?token=07A73AF725622471204758E7172B19D66B5AB1943E6199EC3408B4A96DCC22ED6EDA0697937AF5F98AF1FDC25F8347BF</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.biotechadv.2019.04.008" target="_blank" >10.1016/j.biotechadv.2019.04.008</a>

Result language

angličtina

Original language name

Engineering enzyme access tunnels

Original language description

Enzymes are efficient and specific catalysts for many essential reactions in biotechnological and pharmaceutical industries. Many times, the natural enzymes do not display the catalytic efficiency, stability or specificity required for these industrial processes. The current enzyme engineering methods offer solutions to this problem, but they mainly target the buried active site where the chemical reaction takes place. Despite being many times ignored, the tunnels and channels connecting the environment with the active site are equally important for the catalytic properties of enzymes. Changes in the enzymatic tunnels and channels affect enzyme activity, specificity, promiscuity, enantioselectivity and stability. This review provides an overview of the emerging field of enzyme access tunnel engineering with case studies describing design of all the aforementioned properties. The software tools for the analysis of geometry and function of the enzymatic tunnels and channels and for the rational design of tunnel modifications will also be discussed. The combination of new software tools and enzyme engineering strategies will provide enzymes with access tunnels and channels specifically tailored for individual industrial processes.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

20801 - Environmental biotechnology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2019

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Biotechnology Advances

ISSN

0734-9750

e-ISSN

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Volume of the periodical

37

Issue of the periodical within the volume

6

Country of publishing house

GB - UNITED KINGDOM

Number of pages

13

Pages from-to

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UT code for WoS article

000484647000003

EID of the result in the Scopus database

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