P-Coumaric acid decarboxylase from Lactobacillus plantarum: Structural insights into the active site and decarboxylaction catalytic mechanism

Proteins: Structure, Function and Bioinformatics

Volumn 78, Issue 7, 2010, Pages 1662-1676

  Rodríguez, Héctor ^a   Angulo, Iván ^b,d   De Rivas, Blanca Las ^a   Campillo, Nuria ^c   Páez, Juan A ^c   Muñoz, Rosario ^a   Mancheño, José M ^b  

^a INSTITUTO DE FERMENTACIONES INDUSTRIALES CSIC   (Spain)

^b INSTITUTO DE QUÍMICA FÍSICA ROCASOLANO   (Spain)

^c INSTITUTO DE QUÍMICA MÉDICA   (Spain)

^d SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Catalytic mechanism; Crystal structure; Decarboxylase; P coumaric acid; Phenolic acids

Indexed keywords

CARBON DIOXIDE; CARBOXYLYASE; PARA COUMARIC ACID;

ARTICLE; BINDING SITE; CRYSTALLOGRAPHY; DECARBOXYLATION; ENZYME ASSAY; ENZYME MECHANISM; LACTOBACILLUS PLANTARUM; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; PROTON TRANSPORT; ULTRACENTRIFUGATION;

ALGORITHMS; AMINO ACID SEQUENCE; CARBOXY-LYASES; CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; LACTOBACILLUS PLANTARUM; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; MOLECULAR SEQUENCE DATA; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING; SEQUENCE ALIGNMENT;

LACTOBACILLUS PLANTARUM;

EID: 77951242130     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22684     Document Type: Article

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