About: THE IMPORTANCE OF THE OXYANION HOLE IN ESTER HYDROLYSIS OF ENZYMATIC DEHALOGENTION CATALYZED BY HALOALKANE DEHALOGENASE REVEALED BY QM/MM CALCULATIONS     Goto   Sponge   NotDistinct   Permalink

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Description
  • QMMM výpočty odhalily mechanismus a energetiku druhého kroku hydrolytické dehalogenace katalyzované enzymem halogenalkandehalogenasou LinB. (cs)
  • 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
  • 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 (en)
Title
  • THE IMPORTANCE OF THE OXYANION HOLE IN ESTER HYDROLYSIS OF ENZYMATIC DEHALOGENTION CATALYZED BY HALOALKANE DEHALOGENASE REVEALED BY QM/MM CALCULATIONS
  • THE IMPORTANCE OF THE OXYANION HOLE IN ESTER HYDROLYSIS OF ENZYMATIC DEHALOGENTION CATALYZED BY HALOALKANE DEHALOGENASE REVEALED BY QM/MM CALCULATIONS (en)
  • Význam oxyaniontové díry při esterové hydrolýze enzymové dehalogenase katalyzované halogenalkandehalogenasou odhalený QMMM výpočty (cs)
skos:prefLabel
  • THE IMPORTANCE OF THE OXYANION HOLE IN ESTER HYDROLYSIS OF ENZYMATIC DEHALOGENTION CATALYZED BY HALOALKANE DEHALOGENASE REVEALED BY QM/MM CALCULATIONS
  • THE IMPORTANCE OF THE OXYANION HOLE IN ESTER HYDROLYSIS OF ENZYMATIC DEHALOGENTION CATALYZED BY HALOALKANE DEHALOGENASE REVEALED BY QM/MM CALCULATIONS (en)
  • Význam oxyaniontové díry při esterové hydrolýze enzymové dehalogenase katalyzované halogenalkandehalogenasou odhalený QMMM výpočty (cs)
skos:notation
  • RIV/61989592:15310/06:00004902!RIV08-MSM-15310___
http://linked.open.../vavai/riv/strany
  • L2.13
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(LC512), Z(MSM6198959216)
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 479056
http://linked.open...ai/riv/idVysledku
  • RIV/61989592:15310/06:00004902
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • QMMM; CP; ADMP; haloalkan dehalogenase; oxyanion hole (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...ontrolniKodProRIV
  • [F3E0BEC1DE37]
http://linked.open...i/riv/mistoVydani
  • Bratislava
http://linked.open...i/riv/nazevZdroje
  • Proceedings from XX. Biochemický zjazd
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...iv/tvurceVysledku
  • Carloni, Paolo
  • Damborský, Jiří
  • Otyepka, Michal
  • Banáš, Pavel
  • Magistrato, Alessandra
http://linked.open...n/vavai/riv/zamer
number of pages
http://purl.org/ne...btex#hasPublisher
  • Slovenská akadémia vied
https://schema.org/isbn
  • 80-969532-6-5
http://localhost/t...ganizacniJednotka
  • 15310
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