Functional analyses of active site residues of human lysosomal aspartylglucosaminidase: Implications for catalytic mechanism and autocatalytic activation

EMBO Journal

Volumn 15, Issue 12, 1996, Pages 2954-2960

  Tikkanen, Ritva ^a   Riikonen, Aija ^a   Oinonen, Carita ^b   Rouvinen, Juha ^b   Peltonen, Leena ^a  

^a NATIONAL PUBLIC HEALTH INSTITUTE   (Finland)

^b UNIVERSITY OF EASTERN FINLAND   (Finland)

Author keywords

Active site; Autocatalysis; Catalytic mechanism; Crystal structure; Lysosomal hydrolases

Indexed keywords

AMIDE; ASPARAGINE; CELL PROTEIN; GLYCOPROTEIN; MUTANT PROTEIN; N4 (BETA N ACETYLGLUCOSAMINYL)ASPARAGINASE; OLIGOSACCHARIDE; PROTEIN SUBUNIT;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN TERTIARY STRUCTURE;

EID: 0029936212     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00658.x     Document Type: Article

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