Structural characterization of 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA) from Sphingobium chlorophenolicum, a new type of aromatic ring-cleavage enzyme

Molecular Microbiology

Volumn 88, Issue 3, 2013, Pages 523-536

  Hayes, Robert P ^a   Green, Abigail R ^a   Nissen, Mark S ^a   Lewis, Kevin M ^a   Xun, Luying ^a   Kang, Chulhee ^a  

^a WASHINGTON STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2,6 DICHLORO PARA HYDROQUINONE 1,2 DIOXYGENASE; ARGININE; CATECHOL DERIVATIVE; DIOXYGENASE; HISTIDINE; HYDROQUINONE; HYDROQUINONE 1,2 DIOXYGENASE; HYDROXYL GROUP; IRON; PHENOL DERIVATIVE; SOLVENT; THREONINE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIUM; CONTROLLED STUDY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN MOTIF; REACTION ANALYSIS; SITE DIRECTED MUTAGENESIS; SPHINGOBIUM CHLOROPHENOLICUM; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; BINDING SITES; CALORIMETRY; CATALYSIS; CATECHOLS; DIOXYGENASES; FERROUS COMPOUNDS; HYDROQUINONES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; SPHINGOMONADACEAE;

SPHINGOBIUM CHLOROPHENOLICUM;

EID: 84876722705     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12204     Document Type: Article

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