2021
DOI: 10.1016/j.bbrc.2020.11.098
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Crystal structure of the acyl acid amido synthetase GH3-8 from Oryza sativa

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Cited by 10 publications
(16 citation statements)
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“…Nucleotide-binding sites contain three conserved motifs; motifs are found close to the active site and play a key role in efficient catalysis. The overall architecture of the CcGH3 structures predicted in this study was similar to the OsGH3-8 structure reported recently [ 47 ]. This study also reported the identification of a conserved region that could function in nucleotide binding through three motifs in three plant species: O. sativa , A. thaliana , and V. vinifera [ 47 ].…”
Section: Discussionsupporting
confidence: 85%
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“…Nucleotide-binding sites contain three conserved motifs; motifs are found close to the active site and play a key role in efficient catalysis. The overall architecture of the CcGH3 structures predicted in this study was similar to the OsGH3-8 structure reported recently [ 47 ]. This study also reported the identification of a conserved region that could function in nucleotide binding through three motifs in three plant species: O. sativa , A. thaliana , and V. vinifera [ 47 ].…”
Section: Discussionsupporting
confidence: 85%
“…It is suggested that Asp/Glu are the possible amino acid substrates for most of these CcGH3 proteins. The results showed were determined using the crystallographic data previously reported in AtGH3.5, VvGH3.1, and OsGH3.8 [ 45 , 46 , 47 ].…”
Section: Resultsmentioning
confidence: 99%
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“…The inhibition data, along with the kinetic mechanism of the GH3, indicates that KKI binds to IAA binding site of the GH3•ATP complex leading to formation of the ternary stable complex (Westfall et al 2016;Xu et al 2021). Thus, the GH3•ATP•KKI complex would inhibit synthesis of IAA-amino acid conjugates.…”
Section: Inhibitory Activities Of Kki On Recombinant Gh3 Enzymes In Vitromentioning
confidence: 94%