The identity of the active site of oxalate decarboxylase and the importance of the stability of active-site lid conformations

Biochemical Journal

Volumn 407, Issue 3, 2007, Pages 397-406

  Just, Victoria J ^a,b   Burrell, Matthew R ^a   Bowater, Laura ^a   McRobbie, Iain ^a   Stevenson, Clare E M ^a   Lawson, David M ^a   Bornemann, Stephen ^a  

^a JOHN INNES CENTRE   (United Kingdom)

^b SCHOOL OF MEDICAL SCIENCES   (United Kingdom)

Author keywords

Bacillus subtilis; Catalytically active site; Manganese; Oxalate decarboxylase; Oxalate oxidase; Protein crystallography

Indexed keywords

CARBON DIOXIDE; CARBOXYLATION; CATALYST ACTIVITY; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; MANGANESE;

BACILLUS SUBTILIS; CATALYTICALLY ACTIVE SITE; OXALATE DECARBOXYLASE; OXALATE OXIDASE;

ENZYME KINETICS;

CARBOXYLYASE; MANGANESE; OXALIC ACID; OXIDOREDUCTASE; OXALATE DECARBOXYLASE; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS SUBTILIS; CATALYSIS; CONFORMATION; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME STABILITY; HYDROGEN BOND; KINETICS; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; X RAY CRYSTALLOGRAPHY; AMINO ACID SUBSTITUTION; BINDING SITE; CHEMISTRY; COMPARATIVE STUDY; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETICS; METABOLISM; PROTEIN CONFORMATION;

BACILLUS SUBTILIS;

AMINO ACID SUBSTITUTION; BACILLUS SUBTILIS; BINDING SITES; CARBOXY-LYASES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; MANGANESE; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION;

EID: 35649001771     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070708     Document Type: Article

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