Structural basis of enzymatic activity for the ferulic acid decarboxylase (FADase) from Enterobacter sp. Px6-4

PLoS ONE

Volumn 6, Issue 1, 2011, Pages

  Gu, Wen ^a   Yang, Jinkui ^a   Lou, Zhiyong ^b   Liang, Lianming ^a   Sun, Yuna ^c   Huang, Jingwen ^a   Li, Xuemei ^d   Cao, Yi ^a,e   Meng, Zhaohui ^a,f   Zhang, Ke Qin ^a  

^a YUNNAN UNIVERSITY   (China)

^b TSINGHUA UNIVERSITY   (China)

^c INSTITUTE OF BIOPHYSICS   (China)

^d YUNNAN ACADEMY OF TOBACCO SCIENCE   (China)

^e Guizhou Tobacco Research Institute   (China)

^f KUNMING MEDICAL UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; FERULATE DECARBOXYLASE; UNCLASSIFIED DRUG; CARBOXYLYASE; LIGAND; PHENYLACRYLIC ACID DECARBOXYLASE;

ARTICLE; BACTERIAL STRAIN; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DECARBOXYLATION; ENTEROBACTER; ENZYME ACTIVITY; ENZYME STRUCTURE; GENE MUTATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PLASMID; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTON TRANSPORT; RESTRICTION SITE; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; CHEMISTRY; ENZYMOLOGY; METABOLISM; MISSENSE MUTATION; PROTEIN CONFORMATION; X RAY CRYSTALLOGRAPHY;

ENTEROBACTER SP.;

BINDING SITES; CARBOXY-LYASES; CRYSTALLOGRAPHY, X-RAY; ENTEROBACTER; LIGANDS; MUTAGENESIS, SITE-DIRECTED; MUTATION, MISSENSE; PROTEIN BINDING; PROTEIN CONFORMATION;

EID: 79251633326     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0016262     Document Type: Article

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