THE IMPORTANCE OF THE OXYANION HOLE IN ESTER HYDROLYSIS OF ENZYMATIC DEHALOGENTION CATALYZED BY HALOALKANE DEHALOGENASE REVEALED BY QM/MM CALCULATIONS

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F06%3A00004902" target="_blank" >RIV/61989592:15310/06:00004902 - isvavai.cz</a>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

THE IMPORTANCE OF THE OXYANION HOLE IN ESTER HYDROLYSIS OF ENZYMATIC DEHALOGENTION CATALYZED BY HALOALKANE DEHALOGENASE REVEALED BY QM/MM CALCULATIONS

Original language description

Described QM/MM calculation reveals mechanism and energy profile of the second reaction step (ester hydrolysis) of hydrolytic dehalogenation catalyzed by haloalkane dehalogenase LinB. The catalytic triad Asp-His-Asp/Glu is common to all enzymes in hydrolase family and shares some similarities with the catalytic triad Asp-His-Ser of serine proteases. The reaction step studied comprises a general base catalyzed nucleophile ester hydrolysis. The catalytic base (His272 in LinB) accepts proton from the catalytic water molecule attacking the ester intermediate and transfers it to newly formed alcoholate ion. The catalytic base works as a proton carrier. The Glu132 polarizes His272 to become more basic and to accept proton of the catalytic water molecule easily. The reaction proceeds through tetrahedral intermediate, which appears to be metastable at 300 K with an easy backward reaction to the ester intermediate. The hydrolyzed ester forms enzyme?s protonated aspartic acid (Asp108) and a pr

Czech name

Význam oxyaniontové díry při esterové hydrolýze enzymové dehalogenase katalyzované halogenalkandehalogenasou odhalený QMMM výpočty

Czech description

QMMM výpočty odhalily mechanismus a energetiku druhého kroku hydrolytické dehalogenace katalyzované enzymem halogenalkandehalogenasou LinB.

Type

D - Article in proceedings

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

<a href="/en/project/LC512" target="_blank" >LC512: Center for biomolecules and complex molecular systems</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2006

Confidentiality

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

Article name in the collection

Proceedings from XX. Biochemický zjazd

ISBN

80-969532-6-5

ISSN

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e-ISSN

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Number of pages

1

Pages from-to

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Publisher name

Slovenská akadémia vied

Place of publication

Bratislava

Event location

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Event date

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Type of event by nationality

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UT code for WoS article

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