Lys296 and Arg299 residues in the C-terminus of MD-ACO1 are essential for a 1-aminocyclopropane-1-carboxylate oxidase enzyme activity

Journal of Structural Biology

Volumn 156, Issue 3, 2006, Pages 407-420

  Yoo, Ahrim ^a   Seo, Young Sam ^b   Jung, Jin Won ^c   Sung, Soon Kee ^d   Kim, Woo Taek ^b   Lee, Weontae ^b,c   Yang, Dae Ryook ^a  

^a Korea University   (South Korea)

^b Yonsei University   (South Korea)

^c Department of Biochemistry   (South Korea)

^d Biotech Application Team   (South Korea)

Author keywords

1 Aminocyclopropane 1 carboxylate oxidase; C terminus; Comparative modeling; Molecular dynamics; Site directed mutagenesis; Substrate binding

Indexed keywords

1 AMINOCYCLOPROPANE 1 CARBOXYLATE OXIDASE; ARGININE; GLUTAMIC ACID; LYSINE; MD ACO1 ENZYME; OXIDOREDUCTASE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

ARTICLE; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYMOLOGY; NUCLEOTIDE SEQUENCE; PETUNIA; PRIORITY JOURNAL; PROTEIN MOTIF; SITE DIRECTED MUTAGENESIS; STRUCTURAL PROTEOMICS; STRUCTURE ANALYSIS; SURFACE CHARGE; X RAY CRYSTALLOGRAPHY;

AMINO ACID OXIDOREDUCTASES; AMINO ACID SEQUENCE; ANIMALS; ARGININE; BINDING SITES; COMPUTER SIMULATION; KINETICS; LYSINE; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; MUTATION, MISSENSE; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EMBRYOPHYTA; PETUNIA X HYBRIDA;

EID: 33751012679     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2006.08.012     Document Type: Article

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