Involvement of the α-helical and Src homology 3 domains in the molecular assembly and enzymatic activity of human α1,6-fucosyltransferase, FUT8

• Published in: Biochimica et biophysica acta. General subjects Vol. 1864; no. 7; p. 129596
• Main Authors: Ihara, Hideyuki, Okada, Takahiro, Taniguchi, Naoyuki, Ikeda, Yoshitaka
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.07.2020
• Subjects: active sites; catalytic activity; Catalytic Domain; Core fucosylation; crosslinking; dimerization; disulfide bonds; enzyme activity; Fucosyltransferase; Fucosyltransferases - genetics; Fucosyltransferases - metabolism; FUT8; Glycosyltransferase; Glycosyltransferases; Humans; hydrophobic bonding; Models, Molecular; molecular models; mutants; polyacrylamide gel electrophoresis; Protein dimerization; site-directed mutagenesis; Src homology 3 domain; src Homology Domains; Protein dimerization; SH3 domain; SDS-PAGE; FUT8; Glycosyltransferase; Core fucosylation; Src homology 3 domain; Fucosyltransferase; N-glycan; PCR; HPLC

Previous structural analyses showed that human α1,6-fucosyltransferase, FUT8 contains a catalytic domain along with two additional domains, N-terminal α-helical domain and C-terminal Src homology 3 domain, but these domains are unique to FUT8 among glycosyltransferases. The role that these domains p...