Glycosylation by Pichia pastoris decreases the affinity of a family 2a carbohydrate-binding module from Cellulomonas fimi: A functional and mutational analysis

Biochemical Journal

Volumn 358, Issue 2, 2001, Pages 423-430

  Boraston, A B ^a   Warren, R A J ^a   Kilburn, D G ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

Cellulose binding module; Mapping; Mass spectrometry; N linked; Post translational modification

Indexed keywords

ASSOCIATION REACTIONS; BACTERIA; CARBOHYDRATES; CELLULOSE; POLYPEPTIDES;

GLYCOSYLATION;

MUTAGENESIS;

CARBOHYDRATE BINDING PROTEIN; CELLULOSE; GLYCAN DERIVATIVE; MANNOSE; MUTANT PROTEIN; XYLAN ENDO 1,3 BETA XYLOSIDASE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BINDING SITE; CELLULOMONAS; CONTROLLED STUDY; ESCHERICHIA COLI; NONHUMAN; PICHIA PASTORIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN GLYCOSYLATION;

ACTINOMYCETALES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CELLULOSE; DNA MUTATIONAL ANALYSIS; GLYCOSYLATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PICHIA; POLYSACCHARIDES, BACTERIAL; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; STRUCTURE-ACTIVITY RELATIONSHIP; TRANSFORMATION, GENETIC; XYLAN ENDO-1,3-BETA-XYLOSIDASE; XYLOSIDASES;

EID: 0035447070     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3580423     Document Type: Article

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