Structure/functional study of Lewis α3- and α 3/4-fucosyltransferases: The α1,4 fucosylation requires and aromatic residue in the acceptor-binding domain

Glycobiology

Volumn 14, Issue 4, 2004, Pages 347-356

  Dupuy, Fabrice ^a   Germot, Agnès ^a   Julien, Raymond ^a   Maftah, Abderrhman ^a  

^a UNIVERSITÉ DE LIMOGES   (France)

Author keywords

Acceptor substrate specificity; Aromatic amino acid; Conserved peptide motifs; Lewis fucosyltransferase; Site directed mutagenesis

Indexed keywords

ALPHA 1 4 FUCOSYLTRANSFERASE; ALPHA 3 4 FUCOSYLTRANSFERASE; ALPHA 3 FUCOSYLTRANSFERASE; FUCOSE; FUCOSYLTRANSFERASE; GUANOSINE DIPHOSPHATE; RECEPTOR SUBTYPE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME STRUCTURE; ENZYME SUBSTRATE; FUCOSYLATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN VARIANT; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; ENZYME SPECIFICITY; HUMAN; KINETICS; MAMMAL; METABOLISM; MOLECULAR GENETICS; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY;

VERTEBRATA;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; FUCOSE; FUCOSYLTRANSFERASES; HUMANS; KINETICS; MAMMALS; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 2442442971     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/cwh053     Document Type: Article

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