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

Leskovac, V.; Trivić, S.; Popović, M.

Artykuł - szczegóły

Tytuł artykułu

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

Autorzy

Leskovac V. , Trivić S. , Popović M.

Identyfikatory

Warianty tytułu

Języki publikacji

Abstrakty

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

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

Bibliografia

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Typ dokumentu

Bibliografia

Identyfikator YADDA

bwmeta1.element.baztech-article-BUJ6-0007-0071