Homology modeling of the structure of tobacco acetohydroxy acid synthase and examination of the active site by site-directed mutagenesis

Biochemical and Biophysical Research Communications

Volumn 317, Issue 3, 2004, Pages 930-938

  Le, Dung Tien ^a   Yoon, Moon Young ^b   Kim, Young Tae ^c   Choi, Jung Do ^a  

^a Chungbuk National University   (South Korea)

^b Hanyang University   (South Korea)

^c Pukyong National University   (South Korea)

Author keywords

Acetohydroxy acid synthase; Conserved residues; Herbicide resistance; Homology modeling; Multiple alignments; Site directed mutagenesis; Swiss Model; Tobacco

Indexed keywords

ACETOLACTATE SYNTHASE; DIMER; FLAVINE ADENINE NUCLEOTIDE; HERBICIDE; MUTANT PROTEIN; PYRUVIC ACID;

ARTICLE; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME INACTIVATION; ENZYME STRUCTURE; MOLECULAR MODEL; MUTATION; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; RESIDUE ANALYSIS; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; STRUCTURAL HOMOLOGY; TOBACCO; WILD TYPE; X RAY; YEAST;

ACETOLACTATE SYNTHASE; BASE SEQUENCE; BINDING SITES; CIRCULAR DICHROISM; DNA PRIMERS; DNA, PLANT; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; SPECTROPHOTOMETRY, ULTRAVIOLET; TOBACCO; X-RAY DIFFRACTION;

NICOTIANA TABACUM;

EID: 1842740018     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.03.133     Document Type: Article

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