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Institute of Organic Chemistry
and Biochemistry of the CAS

Take the step towards a career in organic chemistry and biochemistry...


All publications
Rutinosidase from <i>Aspergillus niger</i>: crystal structure and insight into the enzymatic activity
Rutinosidase from Aspergillus niger: crystal structure and insight into the enzymatic activity
Petr Pachl
Jana Kapešová
Jiří Brynda
Lada Biedermannová
Helena Pelantová
Pavla Bojarová
Vladimír Křen
Pavlína Řezáčová
Michael Kotík
FEBS Journal 2020 : Early View (2020).
Rutinosidases (α‐L‐rhamnosyl‐β‐D‐glucosidases) catalyze the cleavage of the glycosidic bond between the aglycone and the disaccharide rutinose (α‐L‐rhamnopyranosyl‐(1→6)‐β‐D‐glucopyranose) of specific flavonoid glycosides such as rutin (quercetin 3‐O‐rutinoside). Microbial rutinosidases are part of the rutin catabolic pathway, enabling the microorganism to utilize rutin and related plant phenolic glycosides. Here, we report the first three‐dimensional structure of a rutinosidase determined at 1.27‐Å resolution. The rutinosidase from Aspergillus niger K2 (AnRut), a member of glycoside hydrolase family GH‐5, subfamily 23, was heterologously produced in Pichia pastoris. The X‐ray structure of AnRut is represented by a distorted (β/α)8 barrel fold with its closest structural homologue being an exo‐β‐(1,3)‐glucanase from Candida albicans (CaExg). The catalytic site is located in a deep pocket with a striking structural similarity to CaExg. However, the entrance to the active site of AnRut has been found to be different from that of CaExg – a mostly unstructured section of ~ 40 residues present in CaExg is missing in AnRut, whereas an additional loop of 13 amino acids partially covers the active site of AnRut. NMR analysis of reaction products provided clear evidence for a retaining reaction mechanism of AnRut. Unexpectedly, quercetin 3‐O‐glucoside was found to be a better substrate than rutin, and thus, AnRut cannot be considered a typical diglycosidase. Mutational analysis of conserved active site residues in combination with in silico modeling allowed identification of essential interactions for enzyme activity and helped to reveal further details of substrate binding. The protein sequence of AnRut has been revised.
Electronic States of 2,3-Diamino-1,4-naphthoquinone and Its N-Alkylated Derivatives
Jin Wen
M. Turowski
P. I. Dron
Jakub Chalupský
R. Grotjahn
T. M. Maier
S. M. Fatur
Zdeněk Havlas
J. C. Johnson
M. Kaupp
Josef Michl
Journal of Physical Chemistry C 124 (1): 60-69 (2020).
Simulation of Raman and Raman optical activity of saccharides in solution
Vladimír Palivec
V. Kopecký
Pavel Jungwirth
Petr Bouř
Jakub Kaminský
Hector Martinez-Seara
Physical Chemistry Chemical Physics 22 (4): 1983-1993 (2020).
Antiviral Drug Targets of Single-Stranded RNA Viruses Causing Chronic Human Diseases
Dinesh Dhurvas Chandrasekaran
S. Tamilarasan
K. Rajaram
Evžen Bouřa
Current Drug Targets 21 (2): 105-124 (2020).
Complexation and stability of the fungicide penconazole in the presence of zinc and copper ions
Ishak Kovač
M. Jakl
Jindřich Fanfrlík
Valery Andrushchenko
Jana Jaklová Dytrtová
Rapid Communications in Mass Spectrometry 2020 : Early View (2020).

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