Crystal Structure of ll-Diaminopimelate Aminotransferase from Arabidopsis thaliana: A Recently Discovered Enzyme in the Biosynthesis of l-Lysine by Plants and Chlamydia

Journal of Molecular Biology

Volumn 371, Issue 3, 2007, Pages 685-702

  Watanabe, Nobuhiko ^a   Cherney, Maia M ^a   van Belkum, Marco J ^a   Marcus, Sandra L ^a   Flegel, Mitchel D ^a   Clay, Matthew D ^a   Deyholos, Michael K ^a   Vederas, John C ^a   James, Michael N G ^a  

^a UNIVERSITY OF ALBERTA   (Canada)

Author keywords

aminotransferase; Arabidopsis thaliana; diaminopimelate; lysine biosynthesis; pyridoxal 5 phosphate

Indexed keywords

AMINOTRANSFERASE; DIAMINOPIMELIC ACID; GLUTAMIC ACID; MALIC ACID; PICOLINIC ACID DERIVATIVE; TETRAHYDRODIPICOLINIC ACID; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARABIDOPSIS; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CHLAMYDIA; CONTROLLED STUDY; CRYSTAL STRUCTURE; DNA SEQUENCE; ENZYME STRUCTURE; ENZYME SYNTHESIS; ESCHERICHIA COLI; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; SEQUENCE ALIGNMENT; SPECTRAL SENSITIVITY;

ARABIDOPSIS THALIANA; BACTERIA (MICROORGANISMS); CHLAMYDIA; CHLAMYDIA SP.; ESCHERICHIA COLI;

EID: 34447618073     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.05.061     Document Type: Article

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