L,L-diaminopimelate aminotransferase from chlamydomonas reinhardtii: A target for algaecide development

PLoS ONE

Volumn 6, Issue 5, 2011, Pages

  Dobson, Renwick C J ^a,b   Girón, Irma ^c   Hudson, André O ^c  

^a UNIVERSITY OF MELBOURNE   (Australia)

^b UNIVERSITY OF CANTERBURY   (New Zealand)

^c ROCHESTER INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AMINOTRANSFERASE; DIAMINOPIMELIC ACID; DIMER; DIPICOLINIC ACID; LEVO,LEVO DIAMINOPIMELATE AMINOTRANSFERASE; LYSINE; MONOMER; PYRIDOXAL 5 PHOSPHATE; TETRAHYDRODIPICOLINIC ACID; UNCLASSIFIED DRUG; 2,3,4,5 TETRAHYDRO 2,6 PYRIDINEDICARBOXYLIC ACID; 2,3,4,5-TETRAHYDRO-2,6-PYRIDINEDICARBOXYLIC ACID; ALGAL PROTEIN; L,L DIAMINOPIMELATE AMINOTRANSFERASE, CHLAMYDOMONAS REINHARDTII; L,L-DIAMINOPIMELATE AMINOTRANSFERASE, CHLAMYDOMONAS REINHARDTII; PESTICIDE; PYRIDINE DERIVATIVE;

ALGAL GROWTH; ARABIDOPSIS; ARTICLE; AUXOTROPHY; CHLAMYDOMONAS REINHARDTII; CONTROLLED STUDY; CRYSTALLIZATION; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ESCHERICHIA COLI; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; ORTHOLOGY; PLANT DEVELOPMENT; PROTEIN TARGETING; SIGNAL TRANSDUCTION; BIOCATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; DRUG EFFECT; ENZYMOLOGY; GENETIC COMPLEMENTATION; GENETICS; GROWTH, DEVELOPMENT AND AGING; KINETICS; METABOLISM; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; PROTEIN TERTIARY STRUCTURE; SOLUTION AND SOLUBILITY; X RAY CRYSTALLOGRAPHY;

ALGAE; ANIMALIA; ARABIDOPSIS; BACTERIA (MICROORGANISMS); CHLAMYDOMONAS REINHARDTII;

ALGAL PROTEINS; BIOCATALYSIS; CATALYTIC DOMAIN; CHLAMYDOMONAS REINHARDTII; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; DIAMINOPIMELIC ACID; ESCHERICHIA COLI; GENETIC COMPLEMENTATION TEST; KINETICS; MODELS, MOLECULAR; MUTATION; PESTICIDES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; PYRIDINES; SOLUTIONS; SUBSTRATE SPECIFICITY; TRANSAMINASES;

EID: 79957521261     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0020439     Document Type: Article

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