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http://yadda.icm.edu.pl:80/baztech/element/bwmeta1.element.baztech-article-BUJ6-0007-0071

Czasopismo

Polish Journal of Chemistry

Tytuł artykułu

Short Hydrogen Bonds in the Catalytic Mechanism of Alcohol and Lactate Dehydrogenases

Autorzy Leskovac, V.  Trivić, S.  Popović, M. 
Treść / Zawartość
Warianty tytułu
Języki publikacji EN
Abstrakty
EN The survey of crystallographic data from the ProteinData Bank for 63 enzyme complexes with substrates indicates the presence of many short hydrogen bonds in the active site of alcohol (EC 1.1.1.1) and lactate (EC 1.1.1.27) dehydrogenases, which are formed between the substrate, or substrate analog, and the acid-base catalyst in enzyme. In the case of alcohol dehydrogenase enzymes, the short hydrogen bonds are clustering in the active site exactly at the bond-breaking position between the substrate and the acid-base catalyst in enzyme, with the frequency of 70-100%. In lactate dehydrogenase enzymes, this frequency is much lower and amounts to 15-30%. This result strongly suggests that the active site of alcohol dehydrogenases is designed to bind the substrate by short hydrogen bonds exactly at the bond-breaking position.
Słowa kluczowe
EN alcohol dehydrogenase   lactate dehydrogenase   short hydrogen bonds  
Wydawca Polskie Towarzystwo Chemiczne
Czasopismo Polish Journal of Chemistry
Rocznik 2006
Tom Vol. 80, nr 12
Strony 1925--1943
Opis fizyczny Bibliogr.
Twórcy
autor Leskovac, V.
autor Trivić, S.
autor Popović, M.
  • Faculty of Technology Novi Sad, University of Novi Sad, 21000 Novi Sad, Serbia
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