Structure and Mechanism of HpcH: A Metal Ion Dependent Class II Aldolase from the Homoprotocatechuate Degradation Pathway of Escherichia coli

Journal of Molecular Biology

Volumn 373, Issue 4, 2007, Pages 866-876

  Rea, Dean ^a   Fülöp, Vilmos ^a   Bugg, Timothy D H ^b   Roper, David I ^a  

^a UNIVERSITY OF WARWICK   (United Kingdom)

^b UNIVERSITY OF WARWICK   (United Kingdom)

Author keywords

aromatic degradation; Catalytic Mechanism; Crystal Structure; homoprotocatechuate; ldolase

Indexed keywords

2 DEHYDRO 3 DEOXYGALACTARATE ALDOLASE; 3,4 DIHYDROXYPHENYLACETIC ACID; 4 HYDROXY 2 OXO HEPTANE 1,7 DIOATE ALDOLASE; ARGININE; ESCHERICHIA COLI PROTEIN; FRUCTOSE BISPHOSPHATE ALDOLASE; HISTIDINE; MAGNESIUM; METAL ION; OXAMIC ACID; UNCLASSIFIED DRUG;

ARTICLE; COMPARATIVE STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; MICROBIAL DEGRADATION; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS;

ESCHERICHIA COLI;

EID: 34848891771     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.06.048     Document Type: Article

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