Role of CH/pi interactions in substrate binding by Escherichia coli ß-galactosidase

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F04%3A00012882" target="_blank" >RIV/60461373:22330/04:00012882 - isvavai.cz</a>

Result on the web

—

DOI - Digital Object Identifier

—

Result language

angličtina

Original language name

Role of CH/pi interactions in substrate binding by Escherichia coli ß-galactosidase

Original language description

Interactions between carbohydrates and aromatic amino-acid residues are often observed in structures of carbohydrate-protein complexes. They are characterized by an orientation of the pyranose or furanose ring parallel with the aromatic ring of amino-acid residues. An important role in the formation of these complexes is supposed to be played by CH/pi interactions. This paper presents an ab initio quantum chemistry study of CH/pi interactions between beta-galactosidase from E. coli and its substrates and products. The energy stabilizing the interaction between Trp999 residue and substrate bound in the shallow binding mode was calculated at the MP2/6-31+G(d) level as 5.2kcalmol(-1) for the glucose moiety of allolactose, 2.4kcalmol(-1) for the galactosemoiety of allolactose and 5.0kcalmol(-1) for the glucose moiety of lactose. The energy stabilizing the interaction between Trp568 residue and galactose in the deep binding mode was calculated as 2.7kcalmol(-1). Interaction energies at the

Czech name

Úloha CH/pi interakcí při vazbě substrátu v ß-galaktosidase z Escherichia coli

Czech description

Úloha CH/pi interakcí při vazbě substrátu v ß-galaktosidase z Escherichia coli

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

—

Project

<a href="/en/project/GA204%2F02%2F0843" target="_blank" >GA204/02/0843: Complex cold adaptation study of enzymes on molecular level and their application in biotechnology</a><br>

Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2004

Confidentiality

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

Name of the periodical

Carbohydrate Research

ISSN

0008-6215

e-ISSN

—

Volume of the periodical

339

Issue of the periodical within the volume

13

Country of publishing house

BE - BELGIUM

Number of pages

5

Pages from-to

2275-2280

UT code for WoS article

—

EID of the result in the Scopus database

—