Engineering enzyme access tunnels

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/00216224:14310/19:00113351

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

Engineering enzyme access tunnels

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Engineering enzyme access tunnels

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

20801 - Environmental biotechnology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

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

Rok uplatnění

2019

Kód důvěrnosti údajů

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

Název periodika

Biotechnology Advances

ISSN

0734-9750

e-ISSN

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Svazek periodika

37

Číslo periodika v rámci svazku

6

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

13

Strana od-do

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Kód UT WoS článku

000484647000003

EID výsledku v databázi Scopus

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