0355844 20240111140752.920110308235959.9 000282750300009 10.1093/glycob/cwq105 10 s. cav_un_epca*02566730959-66582011 (2010)1410-1419Oxford University Press α-N-acetylgalactosaminidase α-galactosidase Aspergillus niger substrate binding molecular modeling cav_un_auth*0269444 Kulik Natallia Oddělení struktury a funkce proteinů Department of Structure and Function of Proteins UEK-B Ústav výzkumu globální změny AV ČR, v. v. i. cav_un_auth*0270141 Weignerová L. CZ cav_un_auth*0241929 Filipi Tomáš 114 - Laboratoř biotrasformací 114 - Laboratory of Biotransformation MBU-M Mikrobiologický ústav AV ČR, v. v. i. cav_un_auth*0104712 Pompach Petr 113 - Laboratoř charakterizace molekulární struktury 113 - Laboratory of  Molecular Structure Characterization MBU-M Laboratory of Structural Biology and Cell Signalization Mikrobiologický ústav AV ČR, v. v. i. cav_un_auth*0265032 Novák Petr Stochastická informatika Department of Stochastic Informatics SI SI UTIA-B Ústav teorie informace a automatizace AV ČR, v. v. i. cav_un_auth*0269630 Mrázek H. CZ cav_un_auth*0247364 Slámová Kristýna 114 - Laboratoř biotrasformací 114 - Laboratory of Biotransformation MBU-M Laboratory of Biotransformation Mikrobiologický ústav AV ČR, v. v. i. cav_un_auth*0016491 Bezouška K. CZ cav_un_auth*0104590 Křen Vladimír 114 - Laboratoř biotrasformací 114 - Laboratory of Biotransformation MBU-M Laboratory of Biotransformation Mikrobiologický ústav AV ČR, v. v. i. cav_un_auth*0106027 Ettrich Rüdiger Oddělení struktury a funkce proteinů Department of Structure and Function of Proteins UEK-B Ústav výzkumu globální změny AV ČR, v. v. i. LC06010 GA MŠk CZ cav_un_auth*0219067 GAP207/10/1934 GA ČR cav_un_auth*0263478 GAP207/10/1040 GA ČR cav_un_auth*0263331 GA303/09/0477 GA ČR cav_un_auth*0252876 GAP207/10/0321 GA ČR cav_un_auth*0263330 CEZ:AV0Z60870520 CEZ:AV0Z50200510 CEZ:AV0Z10750506 Two genes in the genome of Aspergillus niger, aglA and aglB, have been assigned to encode for α-d-galactosidases variant A and B. However, analyses of primary and 3D structures based on structural models of these two enzymes revealed significant differences in their active centers suggesting important differences in their specificity for the hydrolyzed carbohydrates. To test this unexpected finding, a large screening of libraries from 42 strains of filamentous fungi succeeded in identifying an enzyme from A. niger CCIM K2 that exhibited both α-galactosidase andα-N-acetylgalactosaminidase activities, with the latter activity predominating. The enzyme protein was sequenced, and its amino acid sequence could be unequivocally assigned to the enzyme encoded the aglA gene. Enzyme activity measurements and substrate docking clearly demonstrated the preference of the identified enzyme for α-N-acetyl-d-galactosaminide over α-d-galactoside. 2011 CE 10 4 A 4a 20231122134433.4 http://hdl.handle.net/11104/0194522 BIOCHEMISTRYMOLECULARBIOLOGY 4.268 1.213 6.5 0.01679 1.399 6010 141 1.829 Q1 59.514 65.909 Q2 Q1 2010 Soubory v repozitáři: Glycobiology_Final.pdf 000282750300009 WOS 1575 cav_un_epca*0256673 Glycobiology 0959-6658 1460-2423 Roč. 20 č. 11 2010 1410 1419 Oxford University Press