Structural insights of the MenD from Escherichia coli reveal ThDP affinity

Biochemical and Biophysical Research Communications

Volumn 380, Issue 4, 2009, Pages 797-801

  Priyadarshi, Amit ^a,b   Saleem, Yasar ^a   Nam, Ki Hyun ^b   Kim, Key Sun ^a   Park, Sam Yong ^c   Kim, Eunice EunKyeong ^a   Hwang, Kwang Yeon ^b  

^a Korea Institute of Science and Technology   (South Korea)

^b Korea University   (South Korea)

^c YOKOHAMA CITY UNIVERSITY   (Japan)

Author keywords

Decarboxylase; Menaquinone; MenD; Oxoglutarate; ThDP; Transferase

Indexed keywords

2 SUCCINYL 5 ENOLPYRUVYL 6 HYDROXY 3 CYCLOHEXADIENE 1 CARBOXYLATE; BACTERIAL ENZYME; COCARBOXYLASE; DIMER; NUCLEOTIDE; OXOGLUTARATE DEHYDROGENASE; PYRUVATE OXIDASE; TETRAMER; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; BINDING SITE; CIRCULAR DICHROISM; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME CONFORMATION; ESCHERICHIA COLI; GEL FILTRATION; HYDROGEN BOND; ISOTHERMAL TITRATION CALORIMETRY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN STABILITY; X RAY DIFFRACTION;

DIMERIZATION; ENZYME STABILITY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; NUCLEOTIDYLTRANSFERASES; PROTEIN CONFORMATION; PROTEIN SUBUNITS; PYRUVATE OXIDASE; X-RAY DIFFRACTION;

ESCHERICHIA COLI;

EID: 60849134816     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.01.168     Document Type: Article

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