2006
DOI: 10.1016/j.jsb.2006.08.012
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Lys296 and Arg299 residues in the C-terminus of MD-ACO1 are essential for a 1-aminocyclopropane-1-carboxylate oxidase enzyme activity

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Cited by 27 publications
(34 citation statements)
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References 47 publications
(80 reference statements)
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“…1b). Because PnACO1 contains motifs that are evolutionarily conserved and characteristic of ACC oxidases and these motifs are located within the Lys and Arg residues essential for protein activity (Yoo et al 2006) (Fig. 1a), it can be suspected that this gene encodes for a functional enzymatic protein.…”
Section: Discussionmentioning
confidence: 99%
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“…1b). Because PnACO1 contains motifs that are evolutionarily conserved and characteristic of ACC oxidases and these motifs are located within the Lys and Arg residues essential for protein activity (Yoo et al 2006) (Fig. 1a), it can be suspected that this gene encodes for a functional enzymatic protein.…”
Section: Discussionmentioning
confidence: 99%
“…1a). Based on a comparison between the deduced PnACO1 amino acid sequence and ACC oxidase sequences from other plant species, it was found that the PnACO1 protein, too, contains characteristic motifs: a cofactor binding one (Hsp177-X-Asp179-X(54)-Hsp234) and a co-substrate binding one (Arg244-X-Ser246) (Yoo et al 2006). However, at the C-terminus of the PnACO1 protein, an amino acid sequence was identified that was evolutionarily conserved and characteristic of ACC oxidases, containing the Lys and Arg residues essential for enzymatic activity (positions 294-301).…”
Section: Isolation Of Cdna For the Acc Oxidasementioning
confidence: 99%
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“…S2d). The predicted LlACO sequence and ACC oxidases from other plant species were compared and it was found that the LlACO protein also included conserved motifs: a cofactor and a cosubstrate binding [Hsp177-X-Asp179-X(54)-Hsp234 and Arg244-X-Ser246, respectively] [20] (Fig. S2d).…”
Section: Isolation Of Llacs and Llaco Cdnasmentioning
confidence: 99%
“…The amino acid sequence of allele d revealed the presence of a Fe 2+ -binding motif (His-177-X-Asp-179-X(54)-His-234), putative co-substrate hydrogen-binding residues (Arg-244-X-Ser-246), and both Lys-296 and Arg-299 residues in the C-terminal helix, all of which play a key role in the activity of the enzyme (Yoo et al 2006). …”
Section: Cloning and Sequencing Of Allele D Of The Aco1 Genementioning
confidence: 99%