Yu, J CHOI, SO YOUNG Moon, KD Chung, HH Youn, HJ Jeong, S Park, H Schultz, PG 2024-01-21T17:12:41Z 2024-01-21T17:12:41Z 2021-09-03 1998-03 0027-8424 https://pubs.kist.re.kr/handle/201004/143177 Antibodies were generated against the positively charged chair-like glycosidase inhibitor nojirimycin by in vitro immunization. A number of catalytic antibodies were isolated, one of which catalyzes the hydrolysis of p-nitrophenyl beta-D-glucopyranoside 3 with a rate enhancement (k(cat)/kun(cat)) of 10(5) M over the HOAC-catalyzed reaction. The antibody discriminates modifications in the pyranoside ring of substrate 3 at the C2, C4, and the anomeric positions. The pH dependence of the reaction and chemical modification studies suggest the presence of an active-site Asp or Glu residue that may function as a general acid. This study further defines those requirements necessary to generate antibodies that efficiently cleave glycosidic bonds. English NATL ACAD SCIENCES A glycosidase antibody elicited against a chair-like transition state analog by in vitro immunization Article 10.1073/pnas.95.6.2880 1 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.95, no.6, pp.2880 - 2884 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 95 6 2880 2884 N scie scopus 000072596200033 2-s2.0-13144283684 Multidisciplinary Sciences Science & Technology - Other Topics Article CATALYTIC ANTIBODIES BETA-GLUCOSIDASE LYSOZYME HYDROLYSIS INTERMEDIATE INHIBITION catalytic antibody glycosidase chair conformation