Structural and biochemical studies elucidate the mechanism of rhamnogalacturonan lyase from aspergillus aculeatus

Journal of Molecular Biology

Volumn 404, Issue 1, 2010, Pages 100-111

  Jensen, Malene H ^a   Otten, Harm ^a   Christensen, Ulla ^a   Borchert, Torben V ^b   Christensen, Lars L H ^b   Larsen, Sine ^a   Leggio, Leila Lo ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b NOVOZYMES A S   (Denmark)

Author keywords

Active site; Pectin degradation; Polysaccharide lyase family 4; elimination

Indexed keywords

FUNGAL ENZYME; HISTIDINE; LYASE; LYSINE; MUTANT PROTEIN; PECTATE LYASE; POLYSACCHARIDE; RHAMNOGALACTURONAN I; RHAMNOGALACTURONAN LYASE; UNCLASSIFIED DRUG;

ARTICLE; ASPERGILLUS; ASPERGILLUS ACULEATUS; BIODEGRADATION; CATALYSIS; CELL WALL; CONTROLLED STUDY; CRYSTAL; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ELIMINATION REACTION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; GENETIC VARIABILITY; NONHUMAN; PLANT CELL; PRIORITY JOURNAL; REACTION ANALYSIS; WILD TYPE;

ASPERGILLUS ACULEATUS;

EID: 78049451745     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.09.013     Document Type: Article

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