Oxalate decarboxylase and oxalate oxidase activities can be interchanged with a specificity switch of up to 282 000 by mutating an active site lid

Biochemistry

Volumn 46, Issue 43, 2007, Pages 12327-12336

  Burrell, Matthew R ^a   Just, Victoria J ^a   Bowater, Laura ^a   Fairhurst, Shirley A ^a   Requena, Laura ^a   Lawson, David M ^a   Bornemann, Stephen ^a  

^a JOHN INNES CENTRE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITES; DECARBOXYLASE ACTIVITY; DIOXYGEN; OXALATE OXIDASES;

AMINO ACIDS; LIGANDS; MANGANESE; POSITIVE IONS; PROTONATION; REACTION KINETICS;

ENZYME ACTIVITY;

AMINO ACID; CARBOXYLIC ACID; CARBOXYLYASE; GLUTAMIC ACID; LIGAND; MANGANESE; OXALATE DECARBOXYLASE; OXALATE OXIDASE; OXALIC ACID; OXIDOREDUCTASE; OXYGEN; RADICAL; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BACILLUS SUBTILIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SPECIFICITY; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; PROTON TRANSPORT; WILD TYPE;

BINDING SITES; CARBOXY-LYASES; ELECTRON SPIN RESONANCE SPECTROSCOPY; MANGANESE; MUTAGENESIS, SITE-DIRECTED; OXIDOREDUCTASES; SUBSTRATE SPECIFICITY; X-RAY DIFFRACTION;

BACILLUS SUBTILIS;

EID: 35648959174     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700947s     Document Type: Article

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